Anchoring points where the CYTOSKELETON of neighboring cells are connected to each other. They are composed of specialized areas of the plasma membrane where bundles of the ACTIN CYTOSKELETON attach to the membrane through the transmembrane linkers, CADHERINS, which in turn attach through their extracellular domains to cadherins in the neighboring cell membranes. In sheets of cells, they form into adhesion belts (zonula adherens) that go all the way around a cell.
Calcium-dependent cell adhesion proteins. They are important in the formation of ADHERENS JUNCTIONS between cells. Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for neural, and P- for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). Cadherins promote cell adhesion via a homophilic mechanism as in the construction of tissues and of the whole animal body.
Direct contact of a cell with a neighboring cell. Most such junctions are too small to be resolved by light microscopy, but they can be visualized by conventional or freeze-fracture electron microscopy, both of which show that the interacting CELL MEMBRANE and often the underlying CYTOPLASM and the intervening EXTRACELLULAR SPACE are highly specialized in these regions. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p792)
A catenin that binds F-ACTIN and links the CYTOSKELETON with BETA CATENIN and GAMMA CATENIN.
A family of cytoskeletal proteins that play essential roles in CELL ADHESION at ADHERENS JUNCTIONS by linking CADHERINS to the ACTIN FILAMENTS of the CYTOSKELETON.
Cell-cell junctions that seal adjacent epithelial cells together, preventing the passage of most dissolved molecules from one side of the epithelial sheet to the other. (Alberts et al., Molecular Biology of the Cell, 2nd ed, p22)
Desmoplakins are cytoskeletal linker proteins that anchor INTERMEDIATE FILAMENTS to the PLASMA MEMBRANE at DESMOSOMES.
A multi-functional catenin that is highly homologous to BETA CATENIN. Gamma catenin binds CADHERINS and helps link their cytoplasmic tails to ACTIN in the CYTOSKELETON via ALPHA CATENIN. It is also found in DESMOSOMES where it mediates the link between DESMOSOMAL CADHERINS and DESMOPLAKIN.
A multi-functional catenin that participates in CELL ADHESION and nuclear signaling. Beta catenin binds CADHERINS and helps link their cytoplasmic tails to the ACTIN in the CYTOSKELETON via ALPHA CATENIN. It also serves as a transcriptional co-activator and downstream component of WNT PROTEIN-mediated SIGNAL TRANSDUCTION PATHWAYS.
A type of junction that attaches one cell to its neighbor. One of a number of differentiated regions which occur, for example, where the cytoplasmic membranes of adjacent epithelial cells are closely apposed. It consists of a circular region of each membrane together with associated intracellular microfilaments and an intercellular material which may include, for example, mucopolysaccharides. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990; Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
A single-pass transmembrane glycoproteins that mediate CALCIUM-dependent CELL ADHESION and are core components of DESMOSOMES.
Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible.
Connections between cells which allow passage of small molecules and electric current. Gap junctions were first described anatomically as regions of close apposition between cells with a narrow (1-2 nm) gap between cell membranes. The variety in the properties of gap junctions is reflected in the number of CONNEXINS, the family of proteins which form the junctions.
Adherence of cells to surfaces or to other cells.
A group of desmosomal cadherins with cytoplasmic tails that resemble those of classical CADHERINS.
A 195-kDa zonula occludens protein that is distinguished by the presence of a ZU5 domain at the C-terminal of the molecule.
A family of proteins that contain several 42-amino acid repeat domains and are homologous to the Drosophila armadillo protein. They bind to other proteins through their armadillo domains and play a variety of roles in the CELL including SIGNAL TRANSDUCTION, regulation of DESMOSOME assembly, and CELL ADHESION.
A group of desmosomal cadherins with cytoplasmic tails that are divergent from those of classical CADHERINS. Their intracytoplasmic domains bind PLAKOGLOBIN; PLAKOPHILINS; and DESMOPLAKINS.
Surface ligands, usually glycoproteins, that mediate cell-to-cell adhesion. Their functions include the assembly and interconnection of various vertebrate systems, as well as maintenance of tissue integration, wound healing, morphogenic movements, cellular migrations, and metastasis.
A cytoskeletal protein associated with cell-cell and cell-matrix interactions. The amino acid sequence of human vinculin has been determined. The protein consists of 1066 amino acid residues and its gene has been assigned to chromosome 10.
Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.
A MARVEL domain protein that plays an important role in the formation and regulation of the TIGHT JUNCTION paracellular permeability barrier.
Any of several ways in which living cells of an organism communicate with one another, whether by direct contact between cells or by means of chemical signals carried by neurotransmitter substances, hormones, and cyclic AMP.
Orientation of intracellular structures especially with respect to the apical and basolateral domains of the plasma membrane. Polarized cells must direct proteins from the Golgi apparatus to the appropriate domain since tight junctions prevent proteins from diffusing between the two domains.
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
A CALCIUM-dependent adhesion molecule of DESMOSOMES that also plays a role in embryonic STEM CELL proliferation.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.
The synapse between a neuron and a muscle.
Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
Members of the armadillo family of proteins that are found in DESMOSOMES and interact with various proteins including desmocadherins; DESMOPLAKIN; ACTIN FILAMENTS; and KERATINS.
The development of anatomical structures to create the form of a single- or multi-cell organism. Morphogenesis provides form changes of a part, parts, or the whole organism.
Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.
Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
The domestic dog, Canis familiaris, comprising about 400 breeds, of the carnivore family CANIDAE. They are worldwide in distribution and live in association with people. (Walker's Mammals of the World, 5th ed, p1065)
A 43-kDa peptide which is a member of the connexin family of gap junction proteins. Connexin 43 is a product of a gene in the alpha class of connexin genes (the alpha-1 gene). It was first isolated from mammalian heart, but is widespread in the body including the brain.
Established cell cultures that have the potential to propagate indefinitely.
Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
The property of blood capillary ENDOTHELIUM that allows for the selective exchange of substances between the blood and surrounding tissues and through membranous barriers such as the BLOOD-AIR BARRIER; BLOOD-AQUEOUS BARRIER; BLOOD-BRAIN BARRIER; BLOOD-NERVE BARRIER; BLOOD-RETINAL BARRIER; and BLOOD-TESTIS BARRIER. Small lipid-soluble molecules such as carbon dioxide and oxygen move freely by diffusion. Water and water-soluble molecules cannot pass through the endothelial walls and are dependent on microscopic pores. These pores show narrow areas (TIGHT JUNCTIONS) which may limit large molecule movement.
Proteins that take part in the formation or structure of TIGHT JUNCTIONS.
An integral membrane protein that is localized to TIGHT JUNCTIONS, where it plays a role in controlling the paracellular permeability of polarized cells. Mutations in the gene for claudin-1 are associated with Neonatal Ichthyosis-Sclerosing Cholangitis (NISCH) Syndrome.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
A rac GTP-binding protein involved in regulating actin filaments at the plasma membrane. It controls the development of filopodia and lamellipodia in cells and thereby influences cellular motility and adhesion. It is also involved in activation of NADPH OXIDASE. This enzyme was formerly listed as EC
Test for tissue antigen using either a direct method, by conjugation of antibody with fluorescent dye (FLUORESCENT ANTIBODY TECHNIQUE, DIRECT) or an indirect method, by formation of antigen-antibody complex which is then labeled with fluorescein-conjugated anti-immunoglobulin antibody (FLUORESCENT ANTIBODY TECHNIQUE, INDIRECT). The tissue is then examined by fluorescence microscopy.
One or more layers of EPITHELIAL CELLS, supported by the basal lamina, which covers the inner or outer surfaces of the body.
A large family of MONOMERIC GTP-BINDING PROTEINS that are involved in regulation of actin organization, gene expression and cell cycle progression. This enzyme was formerly listed as EC
A group of homologous proteins which form the intermembrane channels of GAP JUNCTIONS. The connexins are the products of an identified gene family which has both highly conserved and highly divergent regions. The variety contributes to the wide range of functional properties of gap junctions.
Fibers composed of MICROFILAMENT PROTEINS, which are predominately ACTIN. They are the smallest of the cytoskeletal filaments.
A zonula occludens protein subtype found in epithelial cell junctions. Several isoforms of zonula occludens-2 protein exist due to use of alternative promoter regions and alternative mRNA splicings.
A desmosomal cadherin that is an autoantigen in the acquired skin disorder PEMPHIGUS FOLIACEUS.
The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.
Differentiation antigens residing on mammalian leukocytes. CD stands for cluster of differentiation, which refers to groups of monoclonal antibodies that show similar reactivity with certain subpopulations of antigens of a particular lineage or differentiation stage. The subpopulations of antigens are also known by the same CD designation.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
The resistance to the flow of either alternating or direct electrical current.
Microscopy using an electron beam, instead of light, to visualize the sample, thereby allowing much greater magnification. The interactions of ELECTRONS with specimens are used to provide information about the fine structure of that specimen. In TRANSMISSION ELECTRON MICROSCOPY the reactions of the electrons that are transmitted through the specimen are imaged. In SCANNING ELECTRON MICROSCOPY an electron beam falls at a non-normal angle on the specimen and the image is derived from the reactions occurring above the plane of the specimen.
Highly specialized EPITHELIAL CELLS that line the HEART; BLOOD VESSELS; and lymph vessels, forming the ENDOTHELIUM. They are polygonal in shape and joined together by TIGHT JUNCTIONS. The tight junctions allow for variable permeability to specific macromolecules that are transported across the endothelial layer.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
A process of complicated morphogenetic cell movements that reorganizes a bilayer embryo into one with three GERM LAYERS and specific orientation (dorsal/ventral; anterior/posterior). Gastrulation describes the germ layer development of a non-mammalian BLASTULA or that of a mammalian BLASTOCYST.
The developmental entity of a fertilized egg (ZYGOTE) in animal species other than MAMMALS. For chickens, use CHICK EMBRYO.
A species of fruit fly much used in genetics because of the large size of its chromosomes.
A member of the Rho family of MONOMERIC GTP-BINDING PROTEINS. It is associated with a diverse array of cellular functions including cytoskeletal changes, filopodia formation and transport through the GOLGI APPARATUS. This enzyme was formerly listed as EC
A RHO GTP-BINDING PROTEIN involved in regulating signal transduction pathways that control assembly of focal adhesions and actin stress fibers. This enzyme was formerly listed as EC
The phenomenon by which dissociated cells intermixed in vitro tend to group themselves with cells of their own type.
A genetically related subfamily of RAP GTP-BINDING PROTEINS that share homology with RAS PROTEINS. They bind to Ras effectors but do not activate them, therefore they may antagonize the effects of RAS PROTEINS. This enzyme was formerly listed as EC
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
A light microscopic technique in which only a small spot is illuminated and observed at a time. An image is constructed through point-by-point scanning of the field in this manner. Light sources may be conventional or laser, and fluorescence or transmitted observations are possible.
Epidermal cells which synthesize keratin and undergo characteristic changes as they move upward from the basal layers of the epidermis to the cornified (horny) layer of the skin. Successive stages of differentiation of the keratinocytes forming the epidermal layers are basal cell, spinous or prickle cell, and the granular cell.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The quality of surface form or outline of CELLS.
A sub-family of RHO GTP-BINDING PROTEINS that is involved in regulating the organization of cytoskeletal filaments. This enzyme was formerly listed as EC
A family of membrane glycoproteins localized to TIGHT JUNCTIONS that contain two extracellular Ig-like domains, a single transmembrane segment, and a cytoplasmic tail of variable length.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
Single pavement layer of cells which line the luminal surface of the entire vascular system and regulate the transport of macromolecules and blood components.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
The external, nonvascular layer of the skin. It is made up, from within outward, of five layers of EPITHELIUM: (1) basal layer (stratum basale epidermidis); (2) spinous layer (stratum spinosum epidermidis); (3) granular layer (stratum granulosum epidermidis); (4) clear layer (stratum lucidum epidermidis); and (5) horny layer (stratum corneum epidermidis).
The epithelium lining the seminiferous tubules composed of primary male germ cells (SPERMATOGONIA) and supporting SERTOLI CELLS. As SPERMATOGENESIS proceeds, the developing germ cells migrate toward the lumen. The adluminal compartment, the inner two thirds of the tubules, contains SPERMATOCYTES and the more advanced germ cells.
Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.
Cells of epithelial origin possessing specialized sensory functions. They include cells that are found in the TASTE BUDS; OLFACTORY MUCOSA; COCHLEA; and NEUROEPITHELIAL BODIES.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Vestibular nucleus lying immediately superior to the inferior vestibular nucleus and composed of large multipolar nerve cells. Its upper end becomes continuous with the superior vestibular nucleus.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action during the developmental stages of an organism.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
Microscopy in which the samples are first stained immunocytochemically and then examined using an electron microscope. Immunoelectron microscopy is used extensively in diagnostic virology as part of very sensitive immunoassays.
A protein complex of actin and MYOSINS occurring in muscle. It is the essential contractile substance of muscle.
A specialized barrier, in the TESTIS, between the interstitial BLOOD compartment and the adluminal compartment of the SEMINIFEROUS TUBULES. The barrier is formed by layers of cells from the VASCULAR ENDOTHELIUM of the capillary BLOOD VESSELS, to the SEMINIFEROUS EPITHELIUM of the seminiferous tubules. TIGHT JUNCTIONS form between adjacent SERTOLI CELLS, as well as between the ENDOTHELIAL CELLS.
Supporting cells projecting inward from the basement membrane of SEMINIFEROUS TUBULES. They surround and nourish the developing male germ cells and secrete ANDROGEN-BINDING PROTEIN and hormones such as ANTI-MULLERIAN HORMONE. The tight junctions of Sertoli cells with the SPERMATOGONIA and SPERMATOCYTES provide a BLOOD-TESTIS BARRIER.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
An epithelial cell line derived from a kidney of a normal adult female dog.
The area covering the terminal portion of ESOPHAGUS and the beginning of STOMACH at the cardiac orifice.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
Specialized areas at the CELL MEMBRANE where a cell attaches to the EXTRACELLULAR MATRIX or other substratum.
A subclass of receptor-like protein tryosine phosphatases that contain multiple extracellular immunoglobulin G-like domains and fibronectin type III-like domains. An additional memprin-A5-mu domain is found on some members of this subclass.
A cultured line of C3H mouse FIBROBLASTS that do not adhere to one another and do not express CADHERINS.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.
An inactive stage between the larval and adult stages in the life cycle of insects.
Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.
An enzyme that catalyzes reversible reactions of a nucleoside triphosphate, e.g., ATP, with a nucleoside monophosphate, e.g., UMP, to form ADP and UDP. Many nucleoside monophosphates can act as acceptor while many ribo- and deoxyribonucleoside triphosphates can act as donor. EC
A PROTEIN-TYROSINE KINASE family that was originally identified by homology to the Rous sarcoma virus ONCOGENE PROTEIN PP60(V-SRC). They interact with a variety of cell-surface receptors and participate in intracellular signal transduction pathways. Oncogenic forms of src-family kinases can occur through altered regulation or expression of the endogenous protein and by virally encoded src (v-src) genes.
Bundles of actin filaments (ACTIN CYTOSKELETON) and myosin-II that span across the cell attaching to the cell membrane at FOCAL ADHESIONS and to the network of INTERMEDIATE FILAMENTS that surrounds the nucleus.
The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)
Preparation for electron microscopy of minute replicas of exposed surfaces of the cell which have been ruptured in the frozen state. The specimen is frozen, then cleaved under high vacuum at the same temperature. The exposed surface is shadowed with carbon and platinum and coated with carbon to obtain a carbon replica.
The subfamily of myosin proteins that are commonly found in muscle fibers. Myosin II is also involved a diverse array of cellular functions including cell division, transport within the GOLGI APPARATUS, and maintaining MICROVILLI structure.
Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.
A microtubule-associated mechanical adenosine triphosphatase, that uses the energy of ATP hydrolysis to move organelles along microtubules toward the plus end of the microtubule. The protein is found in squid axoplasm, optic lobes, and in bovine brain. Bovine kinesin is a heterotetramer composed of two heavy (120 kDa) and two light (62 kDa) chains. EC 3.6.1.-.
Human colonic ADENOCARCINOMA cells that are able to express differentiation features characteristic of mature intestinal cells, such as ENTEROCYTES. These cells are valuable in vitro tools for studies related to intestinal cell function and differentiation.
Specialized cells in the invertebrates that detect and transduce light. They are predominantly rhabdomeric with an array of photosensitive microvilli. Illumination depolarizes invertebrate photoreceptors by stimulating Na+ influx across the plasma membrane.
A gene silencing phenomenon whereby specific dsRNAs (RNA, DOUBLE-STRANDED) trigger the degradation of homologous mRNA (RNA, MESSENGER). The specific dsRNAs are processed into SMALL INTERFERING RNA (siRNA) which serves as a guide for cleavage of the homologous mRNA in the RNA-INDUCED SILENCING COMPLEX. DNA METHYLATION may also be triggered during this process.
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.
A ubiquitously-expressed claudin subtype that acts as a general barrier-forming protein in TIGHT JUNCTIONS. Elevated expression of claudin-3 is found in a variety of tumor cell types, suggesting its role as a therapeutic target for specific ANTINEOPLASTIC AGENTS.
Enzymes that recognize CRUCIFORM DNA structures and introduce paired incisions that help to resolve the structure into two DNA helices.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
A protein factor that regulates the length of R-actin. It is chemically similar, but immunochemically distinguishable from actin.
A method used to study the lateral movement of MEMBRANE PROTEINS and LIPIDS. A small area of a cell membrane is bleached by laser light and the amount of time necessary for unbleached fluorescent marker-tagged proteins to diffuse back into the bleached site is a measurement of the cell membrane's fluidity. The diffusion coefficient of a protein or lipid in the membrane can be calculated from the data. (From Segen, Current Med Talk, 1995).
Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.
A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.
An anchoring junction of the cell to a non-cellular substrate. It is composed of a specialized area of the plasma membrane where bundles of the ACTIN CYTOSKELETON terminate and attach to the transmembrane linkers, INTEGRINS, which in turn attach through their extracellular domains to EXTRACELLULAR MATRIX PROTEINS.
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
An abnormal extension of a gingival sulcus not accompanied by the apical migration of the epithelial attachment.
A form of fluorescent antibody technique commonly used to detect serum antibodies and immune complexes in tissues and microorganisms in specimens from patients with infectious diseases. The technique involves formation of an antigen-antibody complex which is labeled with fluorescein-conjugated anti-immunoglobulin antibody. (From Bennington, Saunders Dictionary & Encyclopedia of Laboratory Medicine and Technology, 1984)
Property of membranes and other structures to permit passage of light, heat, gases, liquids, metabolites, and mineral ions.
Catalyzes the ATP-dependent PHOSPHORYLATION of GMP to generate GDP and ADP.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
A claudin subtype that is found localized to TIGHT JUNCTIONS in VASCULAR ENDOTHELIAL CELLS. The protein was initially identified as one of several proteins which are deleted in VELOCARDIOFACIAL SYNDROME and may play an important role in maintaining the integrity of the BLOOD-BRAIN BARRIER.
Electron microscopy in which the ELECTRONS or their reaction products that pass down through the specimen are imaged below the plane of the specimen.
Macromolecular complexes formed from the association of defined protein subunits.
Elements of limited time intervals, contributing to particular results or situations.
Endothelial cells that line venous vessels of the UMBILICAL CORD.
A desmosomal cadherin that is an autoantigen in the acquired skin disorder PEMPHIGUS VULGARIS.
Derivatives of PHOSPHATIDIC ACIDS that lack one of its fatty acyl chains due to its hydrolytic removal.
A group of intracellular-signaling serine threonine kinases that bind to RHO GTP-BINDING PROTEINS. They were originally found to mediate the effects of rhoA GTP-BINDING PROTEIN on the formation of STRESS FIBERS and FOCAL ADHESIONS. Rho-associated kinases have specificity for a variety of substrates including MYOSIN-LIGHT-CHAIN PHOSPHATASE and LIM KINASES.
An amino alcohol with a long unsaturated hydrocarbon chain. Sphingosine and its derivative sphinganine are the major bases of the sphingolipids in mammals. (Dorland, 28th ed)
A cell line derived from cultured tumor cells.
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.
The process by which cells convert mechanical stimuli into a chemical response. It can occur in both cells specialized for sensing mechanical cues such as MECHANORECEPTORS, and in parenchymal cells whose primary function is not mechanosensory.
Recording serial images of a process at regular intervals spaced out over a longer period of time than the time in which the recordings will be played back.
A quality of cell membranes which permits the passage of solvents and solutes into and out of cells.
ANIMALS whose GENOME has been altered by GENETIC ENGINEERING, or their offspring.
A large family of transmembrane proteins found in TIGHT JUNCTIONS. They take part in the formation of paracellular barriers and pores that regulate paracellular permeability.
The barrier between capillary blood and alveolar air comprising the alveolar EPITHELIUM and capillary ENDOTHELIUM with their adherent BASEMENT MEMBRANE and EPITHELIAL CELL cytoplasm. PULMONARY GAS EXCHANGE occurs across this membrane.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
Cadherins form the cell-cell junctional structures known as adherens junctions as well as the desmosomes. Cadherins are capable ... The E-cadherin - β-catenin - α-catenin complex is weakly associated to actin filaments. Adherens junctions require significant ... While in the adherens junction, cadherins recruit β-catenin molecules onto their intracellular regions[clarification needed]. β ... In cardiac muscle, beta-catenin forms a complex with N-cadherin at adherens junctions within intercalated disc structures, ...
Nectins are the second major class of transmembrane adhesion molecules at adherens junctions, besides cadherins. Therefore, ... is an adherens junction (AJ) protein, involved in the junction's integrity and stability. The protein was discovered in ... function of PLEKHA7 was is to contribute to integrity and stability of the zonula adherens junctions by linking the E-cadherin/ ... Knock-out of PLEKHA7 results in the loss of PDZD11 from epithelial adherens junctions, and this is rescued by the introduction ...
... -mediated calcium entry is required for thrombin-induced disassembly of VE-cadherin adherens junctions. 2- ... "Pyk2 Phosphorylation of VE-PTP Downstream of STIM1 induced Ca2+ entry Regulates Disassembly of Adherens Junctions". American ... "Proteomic mapping of ER-PM junctions identifies STIMATE as a regulator of Ca(2+) influx". Nature Cell Biology. 17 (10): 1339-47 ...
"MAGI1 recruits Dll1 to cadherin-based adherens junctions and stabilizes it on the cell surface". The Journal of Biological ... The product of this gene may play a role as scaffolding protein at cell-cell junctions. Alternatively spliced transcript ... Laura RP, Ross S, Koeppen H, Lasky LA (May 2002). "MAGI-1: a widely expressed, alternatively spliced tight junction protein". ... Patrie KM (Aug 2005). "Identification and characterization of a novel tight junction-associated family of proteins that ...
"ADAM15 is an adherens junction molecule whose surface expression can be driven by VE-cadherin". Exp. Cell Res. 279 (2): 239-47 ...
Thus, E-cadherin forms adherens junctions that connect the actin cytoskeletons of neighbouring cells. Adherens junctions are ... but polarized membranes are essential for maintaining E-cadherin at adherens junctions. Biology portal Cell polarity Bruce ... All epithelial cells express the transmembrane adhesion molecule E-cadherin, a cadherin which localises most prominently to the ... junction between the apical and lateral membranes. The extra-cellular domains of E-cadherin molecules from neighbouring cells ...
... adherens junctions, desmosomes and gap junctions; N-cadherin is an essential component in adherens junctions, which enables ... N-cadherin, a classical cadherin from the cadherin superfamily, is composed of five extracellular cadherin repeats, a ... In cardiac muscle, N-cadherin is an integral component in adherens junctions residing at intercalated discs, which function to ... N-cadherin appears at cell-cell junctions prior to gap junction formation, and is critical for normal myofibrillogenesis. ...
Adherens junctions bind cells together by linking cadherin transmembrane protein complexes of adjacent cells to the ... The entosis process in cancer cells is mediated via E-cadherin and P-cadherin. Since cadherins usually create homolytic cell to ... The process is initiated when epithelial cells form adherens junctions , this is followed by the generation og actomyosin- ... This internalization of one cell by another is dependent on adherens junctions, and is driven by a Rho-dependent process, ...
α-catenin participates in the formation and stabilization of adherens junctions by binding to β-catenin-cadherin complexes in ... are known as adherens junctions and they typically include at least cadherin, β-catenin, and α-catenin. Catenins play roles in ... The exact mechanisms by which α-catenin acts in adherens junctions is still unclear; however, it is likely that α-catenin acts ... For instance, when an epithelial layer is complete and the adherens junctions indicate that the cell is surrounded, β-catenin ...
Adherens junctions are made of cell adhesion molecules from the cadherin family. There are over 100 types of cadherins, ... The most common are E-, N- and P-cadherins. In the adherens junctions of epithelial cells, E-cadherin is the most abundant. ... Of the three types of anchoring junctions, only two are involved in cell-cell interactions: adherens junctions and desmosomes. ... Desmosomes also provide strength and durability to cells and tissues and are located just below adherens junctions. They are ...
This transition occurs through the loss of epithelial cadherin, tight junctions, and adherens junctions on the cell membranes ... The EMT occurs as a result of Wnt signaling, the influence of Sox genes and the loss of E-cadherin from the cell surface. NCCs ... an oncogene associated with the down-regulation of epithelial cadherin. Both formation of the primitive streak and mesenchymal ... additionally require the repression of N-cadherin, and neural cell adhesion molecule. NCCs ingress into the embryo from the ...
... where they commonly stabilize cell-cell junctions known as adherens junctions. Cadherins stabilize adherens junctions through ... Cadherin-1), CDH2 N-cadherin (Cadherin-2), CDH4 R-cadherin (cadherin-4), CDH5 VE-cadherin (cadherin 5, CDH5), CTNND1 ( ... to stabilize E-cadherin-based adherens junctions. PTPmu also dephosphorylates another cell junction protein, connexin 43. The ... Cadherins regulate cell-cell adhesion during development of the body and in adult tissue. Disruption of cadherin proteins, by ...
The junctions between the epidermal cells are of the adherens junction type, formed by transmembrane proteins called cadherins ... Because of the proximity of the neighboring cells and tightness of the junctions, the actin immunofluorescence appears as a ... Inside the cell, the cadherins are linked to actin filaments. In immunofluorescence microscopy, the actin filament network ... Characteristics Physical barrier: Epidermal keratinocytes are tightly linked by cell-cell junctions associated to cytoskeletal ...
... they localize to a cell adhesion structure such as focal adhesion or adherens junction. 2. they directly interact with one of ... Cell-cell adhesion is primarily mediated by cadherin receptors and therefore the adhesome of cell-cell adhesion is referred to ... functional modularity in the adherens junction". Current Opinion in Cell Biology. 36: 32-40. doi:10.1016/ ... Later, with the emergence of the cadherin-catenin-actin structure they were co-opted into the cadhesome. Whittaker, Charles A ...
The encoded protein is associated with VE-cadherin at the adherens junctions of human umbilical vein endothelial cells. ... Glass R, Loesch A, Bodin P, Burnstock G (2002). "P2X4 and P2X6 receptors associate with VE-cadherin in human endothelial cells ...
... gamma-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions". EMBO J ... E-cadherin, N-cadherin, ephrin-B2, or CD44. The gamma secretase complex consists of four individual proteins: PSEN1 (presenilin ... "A CBP binding transcriptional repressor produced by the PS1/epsilon-cleavage of N-cadherin is inhibited by PS1 FAD mutations". ...
p0071 binds E-cadherin at adherens junctions, which are important for maintenance of cell architecture in epithelial tissues, ... interacts with the adherens junction protein p0071 to regulate cell-cell adhesion". PLOS ONE. 7 (11): e47842. Bibcode:2012PLoSO ... Additional supporting evidence includes reduction in E-cadherin expression and increased alveolar apoptosis in lungs from lung- ... April 2014). "Folliculin controls lung alveolar enlargement and epithelial cell survival through E-cadherin, LKB1, and AMPK". ...
"ARVCF localizes to the nucleus and adherens junction and is mutually exclusive with p120(ctn) in E-cadherin complexes". J. Cell ... is a member of the catenin family which play an important role in the formation of adherens junction complexes, which are ... "The armadillo repeat region targets ARVCF to cadherin-based cellular junctions". J. Cell Sci. 113 (22): 4121-35. PMID 11058098 ... "The armadillo repeat region targets ARVCF to cadherin-based cellular junctions". J. Cell Sci. 113 (22): 4121-35. PMID 11058098 ...
A novel actin filament-binding protein with one PDZ domain localized at cadherin-based cell-to-cell adherens junction". The ... an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a ... an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a ... and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions". The Journal of Cell Biology. 144 (5): ...
Adherens junctions are composed primarily of E-cadherin, alpha and beta catenins and other proteins such as actin and myosin. ... E-cadherin is an important transmembrane molecule in creating and facilitating adherens junctions, particularly in epithelial ... Vezatin co-localises with E-cadherin at these cell-cell junctions suggesting that in fact it is involved within adherens ... The adherens junctions in the Sertoli cells is one of the only epithelial cell-cell junction that lacks the expression of ...
Translocation of β-catenin from adherens junctions to the nucleus may lead to a loss of E-cadherin and subsequently to EMT. ... EMT's important feature is the loss of membrane E-cadherin in adherens junctions, where β-catenin may play a significant role. ... "Autoregulation of E-cadherin expression by cadherin-cadherin interactions: the roles of beta-catenin signaling, Slug, and MAPK ... Nuclear β-catenin apparently can directly, transcriptionally activate EMT-associated target genes, such as the E-cadherin gene ...
... epithelial cells adhere to one another as well as the hyaline layer through classic adherens and cadherin junctions. Ingression ... loses adhesion and cadherin, and increase their adhesion to a basal laminal substrate. These processes occur rapidly, over ...
2007). "Type Igamma phosphatidylinositol phosphate kinase modulates adherens junction and E-cadherin trafficking via a direct ...
... is a major cytoplasmic component of both desmosomes and adherens junctions, and is the only known constituent ... Plakoglobin forms distinct complexes with cadherins and desmosomal cadherins. ... Shasby DM, Ries DR, Shasby SS, Winter MC (Jun 2002). "Histamine stimulates phosphorylation of adherens junction proteins and ... Plakoglobin is a cytoplasmic component of desmosomes and adherens junctions structures located within intercalated discs of ...
The nectin-afadin system organizes adherens junctions cooperatively with the cadherin (see MIM 192090)-catenin (see MIM 116805 ... is a human protein of the immunoglobulin superfamily which forms part of adherens junctions. Nectins (e.g., PVRL1; MIM 600644) ... Mueller S, Wimmer E (2003). "Recruitment of nectin-3 to cell-cell junctions through trans-heterophilic interaction with CD155, ...
... tight junctions, adherens junctions, desmosomes, hemidesmosomes, and gap junctions. Tight junctions are a pair of trans- ... They are made up of the integrin (a transmembrane protein) instead of cadherin. They attach the epithelial cell to the basement ... Adherens junctions are a plaque (protein layer on the inside plasma membrane) which attaches both cells' microfilaments. ... Gap junctions connect the cytoplasm of two cells and are made up of proteins called connexins (six of which come together to ...
An Immunoglobulin-like Cell Adhesion Molecule Recruited to Cadherin-based Adherens Junctions through Interaction with Afadin, a ... An Immunoglobulin-like Cell Adhesion Molecule Recruited to Cadherin-based Adherens Junctions through Interaction with Afadin, a ... Yoon M, Spear PG (2002). "Disruption of Adherens Junctions Liberates Nectin-1 To Serve as Receptor for Herpes Simplex Virus and ... is an adhesion molecule found in a wide range of tissues where it localizes in various junctions such as the adherens junction ...
1999). "Nectin/PRR: An Immunoglobulin-like Cell Adhesion Molecule Recruited to Cadherin-based Adherens Junctions through ... This protein is one of the plasma membrane components of adherens junctions. It also serves as an entry for certain mutant ... a Component of Cell-Cell Adherens Junctions". Mol. Cell. Biol. 20 (8): 2865-73. doi:10.1128/MCB.20.8.2865-2873.2000. PMC 85510 ...
Principal interactions of structural proteins are at cadherin-based adherens junction. Actin filaments are linked to α-actinin ... Diagram of a zonula occludens or tight junction, a structure that joins the epithelium of two cells. Actin is one of the ... The head domain of vinculin associates to E-cadherin via α-catenin, β-catenin, and γ-catenin. The tail domain of vinculin binds ... Adhesion of cell epithelia involves the actin cytoskeleton in each of the joined cells as well as cadherins acting as ...
Conversely, cell-cell adhesion via tight and adherens junctions, along with anchoring to extra cellular matrix (ECM) via ... Myosin light chain pulls the actin stress fiber attached to the cadherin, resisting the force of the adjacent cell's cadherin. ... Cunningham KE, Turner JR (July 2012). "Myosin Light Chain Kinase: Pulling the Strings of Epithelial Tight Junction Function". ... regulates epithelial tight junction permeability". The Journal of Biological Chemistry. 279 (53): 55506-13. doi:10.1074/jbc. ...
cell-cell adherens junction. • Z disc. • stress fiber. • filamentous actin. العمليات الحيوية. • response to hypoxia. • ... cadherin binding involved in cell-cell adhesion. • actin binding. • muscle alpha-actinin binding. ...
cell-cell adherens junction. • cell surface. • catenin complex. Biological process. • response to cold. • cell adhesion. • ... This gene encodes a type II classical cadherin from the cadherin superfamily, integral membrane proteins that mediate calcium- ... adherens junction organization. • synaptic transmission, glutamatergic. • homophilic cell adhesion via plasma membrane adhesion ... "Entrez Gene: CDH8 cadherin 8, type 2".. *^ Pagnamenta AT, Khan H, Walker S, Gerrelli D, Wing K, Bonaglia MC, et al. (Jan 2011 ...
cadherin binding. • identical protein binding. Cellular component. • cell-cell adherens junction. • apical junction complex. • ... Cadherin-1 also known as CAM 120/80 or epithelial cadherin (E-cadherin) or uvomorulin is a protein that in humans is encoded by ... E-cadherin (epithelial) is the most well-studied member of the cadherin family. It consists of 5 cadherin repeats (EC1 ~ EC5) ... E-cadherin can sequester β-catenin on the cell membrane by the cytoplasmic tail of E-cadherin. Loss of E-cadherin expression ...
cell-cell adherens junction. Biological process. • cell-cell signaling. • positive regulation of cytokinesis. • positive ... cadherin binding. Cellular component. • cytoplasm. • spindle pole. • membrane. • postsynaptic density. • cell-cell contact zone ... cell-cell junction. • spindle. • desmosome. • cell junction. • midbody. • spindle midzone. • perinuclear region of cytoplasm. • ... Hatzfeld M, Green KJ, Sauter H (2003). "Targeting of p0071 to desmosomes and adherens junctions is mediated by different ...
cell-cell adherens junction. Biological process. • in utero embryonic development. • protein transport. • monocyte ... cadherin binding. • actin filament binding. • microtubule motor activity. • microtubule binding. Cellular component. • myosin ... neuromuscular junction. • cytoplasm. • cytosol. • focal adhesion. • plasma membrane. • stress fiber. • uropod. • immunological ... because of E-cadherin ablation, the inactivation of Myh9 led to the development of tumors recapitulating the features of human ...
Tripathi V, Popescu NC, Zimonjic DB (April 2012). "DLC1 interaction with α-catenin stabilizes adherens junctions and enhances ... Weis WI, Nelson WJ (November 2006). "Re-solving the cadherin-catenin-actin conundrum". J. Biol. Chem. 281 (47): 35593-7. PMID ... A α-catenina participa na formación e estabilización de unións adherentes ao unirse a complexos β-catenina-cadherina na célula. ... Interaccións de proteínas estruturais en unións adherentes baseadas na cadherina. A forma exacta en que as cadherinas se ligan ...
... tight junctions, adherens junctions, desmosomes, hemidesmosomes, and gap junctions. Tight junctions are a pair of trans- ... They are made up of the integrin (a transmembrane protein) instead of cadherin. They attach the epithelial cell to the basement ... Adherens junctions are a plaque (protein layer on the inside plasma membrane) which attaches both cells' microfilaments. ... Cell junctionsEdit. Cell junctions are especially abundant in epithelial tissues. They consist of protein complexes and provide ...
... and vinculin-binding protein localized at cell-cell and cell-matrix adherens junctions". J. Cell Biol. (UNITED STATES) 144 (5 ... 1998). "Vinculin is associated with the E-cadherin adhesion complex". J. Biol. Chem. 272 (51): 32448-53. PMID 9405455. doi: ... Hazan, R B; Kang L; Roe S; Borgen P I; Rimm D L (December 1997). "Vinculin is associated with the E-cadherin adhesion complex ... A vinculina está asociada con unións adherentes e adhesións focais, que son complexos que nuclean os filamentos de actina e ...
Adherens junctionsEdit. Adheren junction showing homophilic binding between cadherins and how catenin links it to actin ... In anchoring junctions between cells such as adherens junctions and desmosomes, the main CAMs present are the cadherins. This ... Adherens junctions mainly function to maintain shape of tissues and hold cells together. In adherens junctions, classical ... as cadherin clusters promotes actin filaments polymerisation which in turn assembles adherens junctions by binding to cadherin- ...
The junctions between the epidermal cells are of the adherens junction type, formed by transmembrane proteins called cadherins ... Cell junctions[edit]. Epidermal cells are tightly interconnected to serve as a tight barrier against the exterior environment. ... Because of the proximity of the neighboring cells and tightness of the junctions, the actin immunofluorescence appears as a ... Inside the cell, the cadherins are linked to actin filaments. In immunofluorescence microscopy, the actin filament network ...
Miller, JR; McClay, DR (1997). "Changes in the pattern of adherens junction-associated beta-catenin accompany morphogenesis in ... Miller, JR; McClay, DR (1997). "Characterization of the Role of Cadherin in Regulating Cell Adhesion during Sea Urchin ...
Epithelial cells are closely connected to each other by tight junctions, gap junctions and adherens junctions, have an apico- ... Loss of E-cadherin is considered to be a fundamental event in EMT. Many transcription factors (TFs) that can repress E-cadherin ... Epithelial cells express high levels of E-cadherin, whereas mesenchymal cells express those of N-cadherin, fibronectin and ... The cells in this tissue express E-cadherin and apical-basal polarity.[32] Since gastrulation is a very rapid process, E- ...
Cell adhesion molecules: Adherens junction *Cadherin. *Desmosome *Desmoglein. *Ion channels: Gap junction/Connexon *Connexin ... "gap junction" and "gap junction plaque" non-interchangeable.[114] In other words, the commonly used term "gap junction" always ... "gap junction" and "gap junction plaque" non-interchangeable as the area of the gap junction plaque may contain proteins other ... Cardiac gap junctions can pharmacologically be opened with rotigaptide.. Neurons[edit]. A gap junction located in neurons is ...
Through its effects on E-cadherin and beta-catenin, which form the adherens junction and promote cell adhesion, NDRG1 also ... "The N-Myc down regulated Gene1 (NDRG1) Is a Rab4a effector involved in vesicular recycling of E-cadherin". PLoS ONE. 2 (9): ... E-cadherin, and mothers against decapentaplegic homolog 4 (SMAD4). ...
cell-cell adherens junction. • cell nucleus. • plasma membrane. • synapse. • central region of growth cone. • glutamatergic ... cadherin binding. • scaffold protein binding. Cellular component. • cytoplasm. • cytosol. • membrane. • kinesin complex. • ... cadherin binding involved in cell-cell adhesion. • RNA binding. • calcium channel regulator activity. • Rab guanyl-nucleotide ...
... in colonic enterocytes strengthens E-cadherin-based adherens junctions to maintain lateral cell-cell contacts and ... "Overexpression of CD97 in intestinal epithelial cells of transgenic mice attenuates colitis by strengthening adherens junctions ... "GPS autoproteolysis is required for CD97 to up-regulate the expression of N-cadherin that promotes homotypic cell-cell ... Ectopic CD97 expression upregulates the expression of N-cadherin and β-catenin in HT1080 fibrosarcoma cells leading to enhanced ...
Sinn HW, Balsamo J, Lilien J, Lin JJ (Sep 2002). "Localization of the novel Xin protein to the adherens junction complex in ... "Loss of cadherin-binding proteins β-catenin and plakoglobin in the heart leads to gap junction remodeling and arrhythmogenesis ... Shasby DM, Ries DR, Shasby SS, Winter MC (Jun 2002). "Histamine stimulates phosphorylation of adherens junction proteins and ... "The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin". Molecular ...
Adherens junctions, also called zonula adherens, are multiprotein complexes formed by proteins of the catenin and cadherin ... Gap junctions Desmosomes Adherens junctions Tight junctions Gap junctions bring the adjacent cells within 2 nanometers of each ... Similar to adherens junctions, the intracellular domains of tight junctions interact with different scaffold proteins, adapter ... its cells are joined securely together by four types of junctions (cell junctions), which can be identified at the ...
"Endocytosis is required for E-cadherin redistribution at mature adherens junctions". PNAS. 106 (17): 7010-15. doi:10.1073/pnas. ... Dimerized cadherins readily bind to their presynaptic cadherin partners. Inhibition of N-cadherin binding via blocking ... N-cadherins are transmembrane proteins expressed in the majority of CNS synapses. N-cadherins are most commonly expressed on ... At basal levels of synaptic activity, N-cadherins are largely monomers and are thus weakly adhesive to cadherins located in the ...
Through SRC, EFS may also negatively regulate expression of E-cadherin at adherens junctions, a function that has been reported ...
Lehtonen S, Lehtonen E, Kudlicka K, Holthöfer H, Farquhar MG (2004). "Nephrin forms a complex with adherens junction proteins ... Ohkubo T, Ozawa M (July 1999). "p120(ctn) binds to the membrane-proximal region of the E-cadherin cytoplasmic domain and is ... "Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells". J. Cell Sci. 110 (17 ... "Cell confluence regulates tyrosine phosphorylation of adherens junction components in endothelial cells". J. Cell Sci. 110 (17 ...
... at the plasma membrane in association with the cadherin/catenin complex is important for the maintenance of adherens junction ... α-catenin and β-catenin in pancreatic acinar cells prior to the dissolution of adherens junctions in a rat model of ... "Protein tyrosine phosphatase kappa and SHP-1 are involved in the regulation of cell-cell contacts at adherens junctions in the ... PTPRK has been shown to interact with: Beta-catenin, E-cadherin (CDH-1), Epidermal growth factor receptor (EGFR), HER2, ...
Intercalated discs are composed of gap junctions, adherens junctions and desmosomes, and are critical for the mechanical and ... Knockdown of LIMP-2 with RNA interference decreased the binding of N-cadherin to the phosphorylated form of beta-catenin, and ... Deficiency of LIMP-2 in mice was also reported to impair cell membrane transport processes and cause pelvic junction ... LIMP-2 has been shown to interact with: N-cadherin. GRCh38: Ensembl release 89: ENSG00000138760 - Ensembl, May 2017 GRCm38: ...
This PTP was shown to function in the regulation of epithelial cell-cell contacts at adherens junctions, as well as in the ... increases beta-catenin-E-cadherin association, and decreases beta-catenin-sensitive transcription". Cancer Res. 61 (4): 1671-7 ...
α-catenin and β-catenin are integral components of adherens junctions, which bind together to produce cadherin-α-catenin-β- ... such as the formation of adherens junctions, tight junctions and focal adhesions. Adherens junctions are a type of cell-cell ... This may serve as a mechanism for how actin is recruited to adherens junctions. Tight junctions, or zona occludens, are the ... Hartsock, Andrea; Nelson, W. James (March 2008). "Adherens and tight junctions: Structure, function and connections to the ...
In human umbilical vein endothelial cells (HUVECs), soluble IQGAP1 associated with VE-cadherin and the catenins, b, y, and a, ... but not N-cadherin. Gene silencing of IQGAP1 by transfection of small interfering RNA (siRNA) wi ... The objectives of the present study were to determine if IQGAP1 associates with components of the endothelial adherens junction ... VE-cadherin was localized at intercellular junctions and less insoluble N-cadherin was present in the cell. These findings ...
We show that a molecular layer seen in crystal structures of E- and N-cadherin ectodomains reported here … ... comprise clusters of type I classical cadherins that bind via extracellular domains extended from opposing cell surfaces. ... Adherens junctions, which play a central role in intercellular adhesion, ... Adherens junctions, which play a central role in intercellular adhesion, comprise clusters of type I classical cadherins that ...
1989) A new 400-kD protein from isolated adherens junctions: its localization at the undercoat of adherens junctions and at ... 1992) Molecular linkage between cadherins and actin filaments in cell-cell adherens junctions. Curr Opin Cell Biol 4:834-839, ... Afadin: A Novel Actin Filament-binding Protein with One PDZ Domain Localized at Cadherin-based Cell-to-Cell Adherens Junction. ... Afadin: A Novel Actin Filament-binding Protein with One PDZ Domain Localized at Cadherin-based Cell-to-Cell Adherens Junction ...
Cadherins are homophilic cell-cell adhesion molecules implicated in many fundamental processes, such as morphogenesis, cell ... Rab35 regulates cadherin-mediated adherens junction formation and myoblast fusion. Team: Membrane Traffic and Cell Division ... They accumulate at cell-cell contact sites and assemble into large macromolecular complexes named adherens junctions (AJs). ... Cadherins are homophilic cell-cell adhesion molecules implicated in many fundamental processes, such as morphogenesis, cell ...
In cadherin‐based adherens junctions (CAJs), the extracellular domains of transmembrane cadherins promote cell-cell adhesion by ... The γ‐secretase‐mediated cleavage of E‐cadherin promotes disassembly of adherens junctions. The molecular weight and ... cadherin intracellular domain and regulates disassembly of adherens junctions. Philippe Marambaud, Junichi Shioi, Geo Serban, ... We observed that in addition to E‐cadherin, two more classic cadherins, N‐ and VE‐cadherins, both of which display high ...
Dejana E, Orsenigo F, Lampugnani MG: The role of adherens junctions and VE-cadherin in the control of vascular permeability. J ... Kam Y, Quaranta V: Cadherin-bound beta-catenin feeds into the Wnt pathway upon adherens junctions dissociation: evidence for an ... Tyrosine phosphorylation of vascular endothelial cadherin (VE-cad) leads to the disruption of endothelial adherens junctions ... Atorvastatin preserves the integrity of endothelial adherens junctions by inhibiting vascular endothelial cadherin tyrosine ...
Adherens junction turnover: Regulating adhesion through cadherin endocytosis, degradation, and recycling. Andrew P. Kowalczyk, ... Adherens junction turnover: Regulating adhesion through cadherin endocytosis, degradation, and recycling. Sub-cellular ... Adherens junction turnover : Regulating adhesion through cadherin endocytosis, degradation, and recycling. / Kowalczyk, Andrew ... Kowalczyk, A. P., & Nanes, B. A. (2012). Adherens junction turnover: Regulating adhesion through cadherin endocytosis, ...
Mbt/PAK4 together with SRC modulates N-Cadherin adherens junctions in the developing Drosophila eye ... Mbt/PAK4 together with SRC modulates N-Cadherin adherens junctions in the developing Drosophila eye ... Mbt/PAK4 together with SRC modulates N-Cadherin adherens junctions in the developing Drosophila eye ... Mbt/PAK4 together with SRC modulates N-Cadherin adherens junctions in the developing Drosophila eye ...
NPRAP colocalized with E-cadherin at adherens junctions. ABP-L-GFP colocalized with NPRAP at these junctions dependent on the ... We conclude that NPRAP in association with cadherin can direct ABP to adherens junctions, but if the NPRAP-cadherin interaction ... Experiments in MDCK cells, which provide a model for cadherins at adherens junctions, demonstrated the formation of cadherin- ... NPRAP draws ABP and GluR2 to adherens junctions. To investigate the role of adherens junctions in the localization of NPRAP-ABP ...
A major formin, mDia1, is shown to be recruited to Adherens Junctions (AJs) by E-Cadherin and RhoA. This leads to the ... What is the role of non-junctional E-cadherin clusters?. Non-junctional E-cadherin clusters play a non-canonical role in ... remodeling of adherens junctions between the apoptotic and neighboring cell surfaces, the contraction of actomyosin structures ... What is the role of non-junctional E-cadherin clusters?. Sruthi Jagannathan2018-03-12T12:57:36+08:30 ...
Adherens Junctions, Adherens junctions Assembly, Cadherin recruitment in adherens junction assembly, Cytoskeleton, Cytoskeleton ... How is cadherin recruited to the adherens junction?steve2018-02-05T16:10:41+08:30 How is cadherin recruited to the adherens ... Actomyosin, Adherens junctions Assembly, Cadherin recruitment in adherens junction assembly, Immunoglobulin superfamily (Ig) ... Cadherin cis interactions during adherens junction initiation. The role of cis interactions between cadherins is less ...
Here the authors show that this is regulated by ubiquitously localized E-cadherin tuning junctional tension and EGFR activity ... In multi-layered epithelia tight junctions (TJ) are confined to the most suprabasal viable layer. ... E-cadherin spatiotemporally coordinates the formation of tension-high adherens junctions, tight junctions, F-actin, and barrier ... adherens junctions (E-cadherin). Note that vinculin-positive junctions are primarily present in the granular layer 2 (SG2). ...
Hypoglycosylated E-cadherin promotes the assembly of tight junctions through the recruitment of PP2A to adherens junctions. ... E-N-cadherin heterodimers define novel adherens junctions connecting endoderm-derived cells. 2011, 195 (5):873-87 J. Cell Biol. ... In epithelial cells, decrease or loss of E-cadherin, the hallmark molecule of adherens junctions (AJs), and increase of N- ... E-N-cadherin heterodimers define novel adherens junctions connecting endoderm-derived cells.. ...
Ezrin regulates E-cadherin-dependent adherens junction assembly through Rac1 activation by Laurence Del Maestro, Alexis ... development and maintenance of cadherin-based adherens junctions requires active Rac1, RhoA, and Cdc42 (Braga et al., 1997, ... and ZO-2 from the lateral TJ membrane without influencing the subjacent adherens junction protein, E-cadherin. In addition, we ... 1 from tight junctions to adherens junctions at high cell confluency. In addition, the expression of �1 integrins caused a ...
... Jon Moulton ... CMTM4 regulates angiogenesis by promoting cell surface recycling of VE-cadherin to endothelial adherens junctions. ... CMTM4 regulates angiogenesis by promoting cell surface recycling of VE-cadherin to endothelial adherens junctions. Angiogenesis ...
... and Dynamin for normal rates of E-cadherin internalization. ... adherens junctions (AJs) maintain the integrity of epithelial ... Cdc42, Par6, and aPKC regulate Arp2/3-mediated endocytosis to control local adherens junction stability Curr Biol. 2008 Nov 11; ...
Adherens junctions, which play a central role in intercellular adhesion, comprise clusters of type I classical cadherins that ... N2 - Adherens junctions, which play a central role in intercellular adhesion, comprise clusters of type I classical cadherins ... AB - Adherens junctions, which play a central role in intercellular adhesion, comprise clusters of type I classical cadherins ... The extracellular architecture of adherens junctions revealed by crystal structures of type i cadherins. Structure. 2011 Feb 9; ...
... tight junctions, cell-cell adherens junctions, and desmosomes (Koch and Franke, 1994). Adherens junctions are specified by ... Since adherens junction proteins engaged in attaching the F-actin to the plasma membrane are detergent-insoluble as discussed ... Actin filaments might be linked to α-catenin and to the adherens junction via α-actinin (Knudsen et al., 1995) or via vinculin ... The findings reported here add new aspects to our present view on cell-cell adherens junctions as outlined in Fig. 10. The ...
Adherens junctions interactions, organism-specific biosystemThe adherens junctions (AJ) are multiprotein complexes that promote ... cadherin-13. Names. H-cadherin (heart). T-cad. T-cadherin. cadherin 13, H-cadherin (heart). heart cadherin. NP_001207417.1. *EC ... Cadherin; Cadherin domain. pfam08758. Location:74 → 159. Cadherin_pro; Cadherin prodomain like. cl09101. Location:636 → 727. E_ ... Cadherin; Cadherin domain. pfam08758. Location:27 → 112. Cadherin_pro; Cadherin prodomain like. cl09101. Location:550 → 641. E_ ...
Adherens junctions interactions, organism-specific biosystemThe adherens junctions (AJ) are multiprotein complexes that promote ... cadherin-5. Names. 7B4 antigen. VE-cadherin. cadherin 5, type 2 (vascular endothelium). cadherin 5, type 2, VE-cadherin ( ... CA; Cadherin repeats. pfam00028. Location:263 → 364. Cadherin; Cadherin domain. pfam01049. Location:633 → 775. Cadherin_C; ... CA; Cadherin repeats. pfam00028. Location:272 → 373. Cadherin; Cadherin domain. pfam01049. Location:635 → 786. Cadherin_C; ...
Adherens junctions (2). * Gene regulation (2). * Cadherins (1). * Cell signalling (1). * Cellular signalling networks (1). ... Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction dynamics and functions *Noboru ... Rights & permissionsfor article Force-dependent allostery of the α-catenin actin-binding domain controls adherens junction ... Nemo kinase phosphorylates β-catenin to promote ommatidial rotation and connects core PCP factors to E-cadherin-β-catenin * ...
N-glycosylation affects the adhesive function of E-cadherin through modifying the composition of adherens junctions (AJs) in ... Autoregulation of E-cadherin expression by cadherin-cadherin interactions: the roles of beta-catenin signaling, Slug, and MAPK ... A Nagafuchi . Molecular architecture of adherens junctions. Curr Opin Cell Biol 2001. 13:600-603. Google Scholar ... E-cadherin, an important member of the cadherin family, is usually expressed in epithelial cells and is involved in calcium- ...
PP6c accumulates at adherens junctions, not tight junctions, co-immunoprecipitates with E-cadherin-catenin complexes without a ... PP6c associates with E-cadherin in adherens junctions and is required to oppose casein kinase-1 to maintain cell surface ... Inducible shRNA knockdown of PP6c dispersed E-cadherin from the cell surface and this response was reversed by chemical ... Signaling pathways regulate E-cadherin function and cellular distribution via phosphorylation of the cytoplasmic region by ...
... barrier dysfunction in a cell death-independent manner with actin stress fiber formation and disruption of adherens junctions ( ... Here, we show that LT reduces total VE-cadherin protein and gene expression but the expression of the key linker protein beta- ... The changes in VE-cadherin expression correlated temporally with the appearance of actin stress fibers and a two-fold increase ... This was accompanied by the restoration of VE-cadherin expression and membrane localization, and attenuation of the LT-induced ...
February 2011). "The extracellular architecture of adherens junctions revealed by crystal structures of type I cadherins". ... cadherin 7, type 2 CDH8 - cadherin 8, type 2 CDH9 - cadherin 9, type 2 (T1-cadherin) CDH10 - cadherin 10, type 2 (T2-cadherin) ... CDH2 - N-cadherin (neural): N-cadherins are found in neurons CDH12 - cadherin 12, type 2 (N-cadherin 2) CDH3 - P-cadherin ( ... Proteopedia Cadherin - view cadherin structure in interactive 3D Cadherin domain in PROSITE The cadherin family The Cadherin ...
CMTM4 regulates angiogenesis by promoting cell surface recycling of VE-cadherin to endothelial adherens junctions Chrifi Ihsan ...
... adherens junctions form.. The binding properties of vertebrate cadherins such as E- and N-cadherin are classically thought to ... 2011 Evolution: structural and functional diversity of cadherin at the adherens junction. J. Cell Biol. 193: 1137-1146. doi: ... 2011 E-N-cadherin heterodimers define novel adherens junctions connecting endoderm-derived cells. J. Cell Biol. 195: 873-887. ... examination of N-cadherin expression in the E-cadherin nonsense mutant, and of E-cadherin expression in the N-cadherin nonsense ...
They preferentially interact with themselves in a homophilic manner in connecting cells; cadherins may thus contribute to the ... cell-cell adherens junction Source: GO_CentralInferred from biological aspect of ancestori*. "Phylogenetic-based propagation of ... IPR039808 Cadherin. IPR002126 Cadherin-like_dom. IPR015919 Cadherin-like_sf. IPR020894 Cadherin_CS. IPR000233 Cadherin_ ... IPR039808 Cadherin. IPR002126 Cadherin-like_dom. IPR015919 Cadherin-like_sf. IPR020894 Cadherin_CS. IPR000233 Cadherin_ ...
desmosomes and adherens junctions. desmosomes = intermediate filaments. adherens junction = actin. cadherins = calcium- ...
2010) Vinculin potentiates E-cadherin mechanosensing and is recruited to actin-anchored sites within adherens junctions in a ... 2012) Vinculin associates with endothelial VE-cadherin junctions to control force-dependent remodeling. J Cell Biol 196:641-652 ... 1998) VE-cadherin and desmoplakin are assembled into dermal microvascular endothelial intercellular junctions: A pivotal role ... 2010) alpha-Catenin as a tension transducer that induces adherens junction development. Nat Cell Biol 12:533-542. ...
  • Experiments in epithelial cells expressing cadherin tagged to a photoconvertible fluropohore for easy tracking, have shown AJs to be highly dynamic structures that continuously turnover cadherin molecules. (
  • In epithelial cells, decrease or loss of E-cadherin, the hallmark molecule of adherens junctions (AJs), and increase of N-cadherin are widely thought to promote carcinoma progression and metastasis. (
  • In epithelial cells, α-, β-, and γ-catenin are involved in linking the peripheral microfilament belt to the transmembrane protein E-cadherin. (
  • To address this question, we used a Förster resonance energy transfer (FRET)-based molecular tension sensor to test the origin and magnitude of tensile forces transmitted through the cytoplasmic domain of E-cadherin in epithelial cells. (
  • CDH1 is a tumour suppressor gene that encodes E-cadherin, a homophilic cell-to-cell adhesion protein that is localised to the adherens junction on the basolateral surface of epithelial cells. (
  • E-Cadherin is the major cadherin in polarized epithelial cells, whereas N-cadherin is expressed mainly by mesenchymal cells, such as myocytes and fibroblasts. (
  • E-cadherin is a well-characterised single-pass transmembrane Type I cadherin that is primarily expressed on epithelial cells and contains a cytoplasmic domain of 150aa and an extracellular domain of 550aa containing five EC repeats, each of approximately 110aa [ 1 , 2 ]. (
  • Adherens junctions uniquely disassemble in uterine epithelial cells to allow the blastocyst to penetrate between epithelial cells. (
  • E-cadherin is a major component of adherens junctions in epithelial cells. (
  • Assembly of the tight junction barrier is dependent upon neighboring epithelial cells binding to one another and forming adherens junctions, but the mechanism for how these processes are linked is poorly understood. (
  • For example, E-cadherin, the prototype and the best-characterized classical cadherin, is expressed primarily in epithelial cells. (
  • Several distinct intercellular junctions connect epithelial cells. (
  • The primary mechanical role of catenins is connecting cadherins to actin filaments, specifically in these adhesion junctions of epithelial cells. (
  • Intercellular contacts between epithelial cells are mediated by morphologically distinct adhesion complexes such as tight junctions, gap junctions, desmosomes, and adherens junctions. (
  • E-cadherin is a well-known homotypic adhesion molecule that mainly expresses in epithelial cells and serves as a suppressor of tumor growth and metastasis ( 1, 2 ). (
  • Unlike the glycoproteins that are required for infection, the protein encoded by CMV US9 plays an accessory role by promoting dissemination of virus across cell-cell junctions of polarized epithelial cells. (
  • In polarized epithelial cells, gpUS9 also accumulated along lateral membranes, colocalizing with cadherin and actin, and was insoluble in Triton X-100, a property shared with proteins that associate with the cytoskeleton. (
  • The herpes simplex virus (HSV) glycoprotein complex gE-gI mediates the spread of viruses between adjacent cells, and this property is especially evident for cells that form extensive cell junctions, e.g., epithelial cells, fibroblasts, and neurons. (
  • gE-gI accumulated at lateral surfaces of the epithelial cells, colocalizing with the adherens junction protein β-catenin but was not found on either the apical or basal plasma membranes and did not colocalize with ZO-1, a component of tight junctions. (
  • Similar localization of gE-gI to cell junctions was observed in HSV-infected epithelial cells. (
  • The reduced cell-to-cell spread of gE or gI mutant viruses was most evident in plaque assays involving cells that form extensive cell junctions, i.e., normal human fibroblasts and epithelial cells, rather than transformed cells. (
  • In vitro studies in simple epithelial cells indicated an essential role for E-cadherin not only in the formation of AJs but also other intercellular contacts, such as desmosomes and tight junctions. (
  • Epithelial cells are attached to each other by E-cadherin, an adherens junction protein. (
  • Formation of the initial membrane contacts between two epithelial cells creates a distinct cell area in which a pool of mobile E-cadherin is sequestered into immobile puncta along membrane contacts. (
  • We demonstrate that c-Jun N-terminal kinase (JNK) responds to substrate stiffness and regulates adherens junction (AJ) formation in epithelial cells in 2D cultures and in 3D tissues in vitro and in vivo. (
  • These findings suggest that a reduction of IQGAP1 positively influences the endothelial barrier by increasing the protein level of VE-cadherin and the interaction of VE-cadherin with the actin cytoskeleton. (
  • Thus, many F-actin- binding proteins appear to serve as linkers of the actin cytoskeleton to the plasma membrane cadherin and integrin. (
  • The PS1/γ‐secretase cleavage dissociates E‐cadherins, β‐catenin and α‐catenin from the cytoskeleton, thus promoting disassembly of the E‐cadherin-catenin adhesion complex. (
  • Rearrangements of the actin cytoskeleton and E-cadherin-based adherens junctions caused by neoplasic transformation change cell-cell interactions. (
  • This positioning necessitates tissue-level polarization of junctions and the cytoskeleton through unknown mechanisms. (
  • For example, apico-basolateral polarity promotes the asymmetric positioning of intercellular junctions and the cytoskeleton within the cell to drive functional barrier formation in simple epithelia 1 . (
  • The intracellular portion of classical cadherins has regulatory proteins that helps the cadherins joining the actin cytoskeleton. (
  • The extracellular domain of classical cadherins forms intercellular bonds with cadherins on neighboring cells, whereas the cytoplasmic domain recruits catenins, which in turn associate with additional cytoskeleton binding and regulatory proteins. (
  • We show that the actomyosin cytoskeleton exerts pN-tensile force on E-cadherin, and that this tension requires the catenin-binding domain of E-cadherin and αE-catenin. (
  • Surprisingly, the actomyosin cytoskeleton constitutively exerts tension on E-cadherin at the plasma membrane regardless of whether or not E-cadherin is recruited to cell-cell contacts, although tension is further increased at cell-cell contacts when adhering cells are stretched. (
  • Our findings thus point to a constitutive role of E-cadherin in transducing mechanical forces between the actomyosin cytoskeleton and the plasma membrane, not only at cell-cell junctions but throughout the cell surface. (
  • Although it is generally thought that cadherins are physically connected to the cytoskeleton through catenins ( 13 ), the cadherin/catenin complex appears to bind poorly to actin in vitro ( 14 , 15 ). (
  • Mechanical coupling between the plasma membrane and the cortical cytoskeleton involves the cadherin cytoplasmic domain ( 24 ). (
  • An adherens junction is defined as a cell junction whose cytoplasmic face is linked to the actin cytoskeleton. (
  • The β -catenin binding domain facilitates interaction of E-cadherin with the actin cytoskeleton via the Cytoplasmic Cell adhesion Complex (CCC), which consists of β -catenin, α -catenin, and, possibly, Epithelial Protein Lost In Neoplasm (EPLIN) [ 4 ] (Figure 2 ). (
  • α-catenin or alpha-catenin binds the cadherin indirectly via β-catenin or plakoglobin and links the actin cytoskeleton with cadherin. (
  • As adhesive proteins, both β -catenin and plakoglobin interact with the cytoplasmic domain of cadherins, thereby tethering the cadherin proteins to the cytoskeleton. (
  • The actin cytoskeleton is a key regulator of barrier structure and function, controlling the assembly and permeability of epithelial adherens and tight junctions. (
  • While the extracellular domain of cadherin induces cell-cell adhesion in the presence of Ca 2+ , an interaction between the cytoplasmic domain of cadherin and the underlying actin cytoskeleton is also required for the construction of tight and compact cell-cell adhesions (for a review, see reference 32 ). (
  • Cadherins mediate cell-cell adhesion through interactions between N-terminal cadherin domains on opposing cell surfaces and by organization of the actin cytoskeleton through α-catenin ( Nelson, 2008 ). (
  • To this end, we have analysed the role of α-Catenin, a key molecule linking E-Cadherin-based adhesion and the actomyosin cytoskeleton, during Drosophila embryonic dorsal closure, by studying a newly developed allelic series. (
  • The name "catenin" was originally selected ('catena' means 'chain' in Latin) because it was suspected that catenins might link cadherins to the cytoskeleton. (
  • β-catenin acts by anchoring the actin cytoskeleton to the junctions, and may possibly aid in contact inhibition signaling within the cell. (
  • Proteins that are associated with the cytoplasmic domain of adhesion molecules such as cadherins and link them to the cytoskeleton. (
  • It has long been recognized that the biology of E-cadherin arises from cooperation between adhesion and the actin cytoskeleton. (
  • Indeed, it has long been appreciated that biochemical and functional links with the actin cytoskeleton play a vital role in cadherin biology. (
  • Intracellularly, E-cadherins are linked to the actin cytoskeleton and to signaling cascades through a multiprotein complex consisting mainly of catenins ( 4 , 46 , 49 ). (
  • In adherens junctions, alpha-catenin links the cadherin-beta-catenin complex to the actin-based cytoskeleton. (
  • On the inside of the cell, cadherin binds to 'adaptor' proteins, which essentially connect the cadherin to a network of protein filaments known as the cytoskeleton. (
  • The cadherin and the cytoskeleton compartments appeared to be separated by an 'interface layer', which contains vinculin, a stretchable protein which has long been implicated in the cell's ability to sense mechanical force. (
  • This elongated form was sufficient to stretch over a distance of 30 nanometres or more, which was the same distance that cadherin was separated from the cytoskeleton. (
  • Normally, E-cadherin locates on the cell surface with its cytosolic domain linking to the actin cytoskeleton through interaction with catenins. (
  • Interendothelial adherens junctions (AJs) that maintain endothelial barrier function are largely composed of vascular endothelial cadherin (VE-cad), an endothelium-specific member of the cadherin family of adhesion proteins. (
  • Cadherins, NPRAP, GRIP, and GluR2 copurified in the fractionation of synaptosomes and the postsynaptic density, two fractions enriched in synaptic proteins. (
  • Thus, the interaction of scaffolding proteins with cadherin-NPRAP complexes may anchor diverse signaling and adhesion molecules at cadherins. (
  • Adherens junctions are specified by transmembrane linker proteins, the cadherins, which mediate the calcium-dependent, homophilic cell-cell adhesion in a wide variety of tissues and species. (
  • Cadherins are a class of type-1 transmembrane proteins, and they are dependent on calcium (Ca2+) ions to function, hence their name. (
  • Cell-cell adhesion is mediated by extracellular cadherin domains, whereas the intracellular cytoplasmic tail associates with numerous adaptors and signaling proteins, collectively referred as the cadherin adhesome. (
  • The adaptor proteins that associate with desmosomal cadherins are plakoglobin (related to β {\displaystyle \beta } -catenin), plakophilins (p120 catenin subfamily), and desmoplakins. (
  • Cadherins are synthesized as polypeptides and undergo many post-translational modifications to become the proteins which mediate cell-cell adhesion and recognition. (
  • Cadherins are calcium-dependent cell adhesion proteins. (
  • Classical cadherins are transmembrane proteins at the core of intercellular adhesion complexes in cohesive metazoan tissues. (
  • Classical cadherins are transmembrane proteins that form intercellular bonds through interactions between their extracellular domains on apposed cells. (
  • Inside the cell E-cadherin binds to catenin, which in turn binds to other proteins in a protein complex with actin filaments Desmosomes connect two cells together structure: thickening of adjacent cell membrane, a pair of attachment plaques, transemembrane protein and tonofilaments. (
  • Adherens junctions are composed of the following proteins: cadherins. (
  • The cadherins are a family of transmembrane proteins that form homodimers in a calcium-dependent manner with other cadherin molecules on adjacent cells. (
  • It appears that the transmission of forces from cellular domains occupied by E-cadherin to F-actin filaments is regulated by the intracellular recruitment and accumulation of a number of effector proteins at sites of cell-cell adhesion ( 27 , 28 ). (
  • In addition, several groups showed that E-cadherin (initially known as uvomorulin) immunoprecipitates contained three distinct proteins, which became known as α -, β -, and γ -catenin [ 14 - 16 ]. (
  • These studies showed that these three catenin proteins, with molecular weights of approximately 102, 88, and 80 kDa, respectively, interacted with the cytoplasmic domain of E-cadherin. (
  • Proteins such as ZO-1, ZO-2, ZO-3, MUPP-1, and PATJ colocalize with claudin proteins and together form tight junctions (Figure 2) . (
  • These proteins form cell−cell junctions (Figure 3), and can facilitate signaling pathways such as AKT, Wnt, and MAPK to govern morphogenesis, tissue homeostasis, and intercellular communication 5. . (
  • Cells bind flexibly to each other when the tips of cadherin proteins on each cell surface form swiveling connections within the cell-cell junctions. (
  • Cadherins are the most crucial membrane proteins for the formation of tight and compact cell-cell contacts. (
  • Among many junctional proteins, cadherins, especially classical cadherins, are the most crucial membrane proteins for the establishment of intercellular adhesions (for reviews, see references 15 and 32 ). (
  • The extracellular regions of these transmembrane proteins mediate intercellular binding, while their cytoplasmic domains are linked to the actin- (adherens junction) or intermediate filament- (desmosome) based cytoskeletons. (
  • the collection of chapters in this book highlight the remarkable diverse biological functions of intercellular junction proteins while also addressing future research directions in this vast and continuously evolving scientific field. (
  • This volume will be of great interest to cell and developmental biologists in addition to others who want to understand how intercellular junction proteins impact development, health and human disease. (
  • The classic cadherins contain a highly conserved cytoplasmic domain that interacts with a family of cytoplasmic proteins called catenins: α-catenin, β-catenin, plakoglobin, and p120 ( 30 , 31 , 36 , 41 ). (
  • Catenins are a family of proteins found in complexes with cadherin cell adhesion molecules of animal cells. (
  • Western blot analysis of P. gingivalis -challenged HOK-16 cells revealed proteolysis of focal contact components (e.g., focal adhesion kinase), adherens junction proteins (e.g., catenins), and adhesion signaling molecules (e.g., the tyrosine kinase SRC). (
  • One of the main protein parts in these machines are the 'cadherin' proteins. (
  • Signalling through adhesion receptors such as integrins and cadherins plays a key role in regulating epidermal function and the Rho family of small GTP-binding proteins play a central role in regulating these adhesion-dependent signaling events. (
  • We recently identified several proteins at the eptithelial junctions as host factors involved in the pathogenesis of one of Staphylococcus aureus major toxins. (
  • Hippo pathway can also be negatively regulated by adherens junction-associated proteins . (
  • To test whether adherens junction proteins are present in the epithelium and the endothelium of corneal equivalents. (
  • Cells from the epithelial and endothelial layers expressed adherens junction proteins, indicating the presence of cell-cell contacts and the existence of polarized morphology of these layers over corneal equivalents. (
  • These functions are fulfilled by tight junctions and associated proteins as well as cell-cell adhesion mechanisms. (
  • The PS1/γ‐secretase system cleaves both the full‐length E‐cadherin and a transmembrane C‐terminal fragment, derived from a metalloproteinase cleavage after the E‐cadherin ectodomain residue Pro700. (
  • This calcium-dependent cell-cell adhesion molecule is comprised of five extracellular cadherin repeats, a transmembrane region and a highly conserved cytoplasmic tail. (
  • Similar to classical cadherins, desmosomal cadherins has a single transmembrane domain, five EC repeats, and an intracellular domain. (
  • The components that build an atypical cadherin are flamingo (seven pass transmembrane) and Dcad102F-like cadherins. (
  • Each cadherin has a small C-terminal cytoplasmic component, a transmembrane component, and the remaining bulk of the protein is extra-cellular (outside the cell). (
  • CADHERINS are a large family of transmembrane glycoproteins that regulate cell affinity. (
  • In this subfamily, all cadherins have an ectodomain possessing five characteristic EC repeats, responsible for their Ca ++ -dependent cell affinity, a transmembrane domain, and a highly conserved cytoplasmic tail that anchors cadherins to the cell cortex through their association with p120 catenin, β-catenin, and α-catenin. (
  • The cadherins, transmembrane adhesion molecules, are found with catenins at adherens junctions (zonula adherens). (
  • The last complex contains E-cadherins, transmembrane cell-cell adhesion receptors, which link adjacent cells via calcium-dependent homophilic interactions between extracellular domains. (
  • Here, we demonstrate that depletion of MarvelD3 , a transmembrane protein of tight junctions, disrupts neural crest formation and, consequently, development of neural crest-derived tissues during Xenopus embryogenesis. (
  • Reduction of IQGAP1 induced an increase and a decrease, respectively, in the protein levels of VE-cadherin and N-cadherin. (
  • A novel actin filament (F-actin)-binding protein with a molecular mass of ∼205 kD (p205), which was concentrated at cadherin-based cell-to-cell adherens junction (AJ), was isolated and characterized. (
  • We named p205 l-afadin (a large splicing variant of AF-6 protein localized at adherens junction) and p190 s-afadin (a small splicing variant of l-afadin). (
  • Here we show that presenilin‐1 (PS1), a protein involved in Alzheimer's disease, controls a γ‐secretase‐like cleavage of E‐cadherin. (
  • The role of protein kinase C (PKC) in induction of endothelial cells adherence junction disruption by exposure of HUVECs to high concentration of glucose was explored. (
  • NPRAP is an ARM repeat protein that binds to the juxtamembrane region of the cadherin intracellular domain. (
  • The protein lacks the cytoplasmic domain characteristic of other cadherins, and so is not thought to be a cell-cell adhesion glycoprotein. (
  • Functioning as a classical cadherin by imparting to cells the ability to adhere in a homophilic manner, this protein plays a role in endothelial adherens junction assembly and maintenance. (
  • VE-cadherin internalization from tensile adherens junctions is inhibited by Pacsin2 protein. (
  • Title: The F-BAR protein pacsin2 inhibits asymmetric VE-cadherin internalization from tensile adherens junctions. (
  • α-Catenin exhibits sequence homologies over three regions to vinculin, another adherens junction protein. (
  • U0126, an inhibitor of extracellular signal-regulated protein kinase (ERK), attenuated the CsA-induced transcriptional repressor SNAI2 (also called Slug) expression and restored E-cadherin expression inhibited by CsA in JEG-3 cells. (
  • Here, we show that LT reduces total VE-cadherin protein and gene expression but the expression of the key linker protein beta-catenin remained unchanged. (
  • The changes in VE-cadherin expression correlated temporally with the appearance of actin stress fibers and a two-fold increase in phosphorylation of the stress fiber-associated protein myosin light chain (p-MLC) and cleavage of Rho-associated kinase-1 (ROCK-1). (
  • Once the cell-cell adhesion between cadherins present in the cell membranes of two different cells has formed, adherens junctions can then be made when protein complexes, usually composed of α-, β-, and γ-catenins, bind to the cytoplasmic portion of the cadherin. (
  • The cell adhesion molecule N-cadherin is enriched at the SC-axon interface and colocalizes with the polarity protein Par-3. (
  • The synthetic lethal relationship between selected protein classes and E-cadherin was characterised by drug sensitivity assays in both the isogenic breast MCF10A cells and CDH1 -isogenic gastric NCI-N87. (
  • N-Cadherin-mediated cell adhesion-activated antiapoptotic protein Akt/PKB and subsequently increased β-catenin and inactivated the proapoptotic factor Bad. (
  • The intercellular space in cell-cell junctions is maintained at 20 nm Adhesive junctions Adherens junctions (or zonula adherens, intermediate junction, or 'belt desmosome'[1]) are protein complexes that occur at cell-cell junctions in epithelial tissues, usually more basal than tight junctions. (
  • E-cadherin is the primary cell adhesion molecule within the epithelium, and loss of this protein is associated with a more aggressive tumour phenotype and poorer patient prognosis in many cancers. (
  • The cadherin family is characterised by the presence of extracellular cadherin (EC) repeats within the ectodomain of the protein, which vary in number within the family. (
  • Adherens junctions (or zonula adherens, intermediate junction, or "belt desmosome") are protein complexes that occur at cell-cell junctions in epithelial and endothelial tissues, usually more basal than tight junctions. (
  • The authors used an elegant approach in which recombinant E-, N-, or P-cadherin ectodomains fused to the Fc of immunoglobulin (E-cad/Fc, N-cad/Fc, or P-cad/Fc) were used for protein mimicry to support islet cell attachment ( Fig. 1 ). (
  • 12 ] demonstrated that this 83 kDa protein was present in both desmosomes and the adherens junction and was given the name plakoglobin. (
  • Protein kinase C regulates endocytosis and recycling of E-cadherin. (
  • In the present study, we investigated the potential role of protein kinase C (PKC) in regulating the trafficking of surface E-cadherin in Madin-Darby canine kidney cells. (
  • Already know your cell junction protein target of interest? (
  • We find that during the growth phase of the dermomyotome sheet, when the orientation of mitotic spindles is parallel to the mediolateral extent of the epithelium, N-cadherin protein is inherited by both daughter cells. (
  • β-Catenin is a 92kDa protein that binds to the cytoplasmic tail of E-Cadherin. (
  • However, binding of E-cadherin to Type I gamma phosphatidylinositol phosphate kinase (PIPKIγ), a protein required for recruitment of E-cadherin to adhesion sites, was blocked by O-GlcNAc glycosylation (O-GlcNAcylation). (
  • An important component of this process is E-cadherin, a single-membrane-spanning protein with a conserved cytoplasmic domain and divergent extracellular regions composed of five cadherin domains separated by interdomain Ca 2+ binding sites ( Gumbiner, 2000 ). (
  • First of all, by binding to cadherin receptor intracellular cytoplasmic tail domains, it can act as an integral component of a protein complex in adherens junctions that helps cells maintain epithelial layers. (
  • Here, the researchers 'mapped' the position and orientation of the protein building blocks of cadherin adhesions. (
  • IFN-γ acts pathogenic by causing a breakdown of the vascular barrier through disruption of the adherens junction protein VE-cadherin. (
  • In the nucleus, E-cadherin was acetylated by CREB-binding protein at Lysine 870 and Lysine 871 in its β-catenin-binding domain, and the acetylation can be reversed by SIRT2. (
  • E-cadherin en- gagement at adherens junction suppresses the nuclear location and activity of YAP by regulating MST1 and 2 activity, or via alpha-catenin by sequestrating 14-3-3 protein complexes within the cytoplasm. (
  • The adherens junction protein N-cadherin was distributed circumferentially at day 1 but began to organize into intercalated disk-like structures by day 6. (
  • The gap junction protein connexin43 followed a similar but delayed pattern relative to N-cadherin. (
  • CD144, also called Cadherin 5, CDH5 or VE-Cadherin is a 140 kDa protein belonging to the cadherin family of cell adhesion molecules which interact homophilically in trans and form lateral interactions in cis. (
  • Our data identify the junctional protein MarvelD3 as an essential regulator of early vertebrate development and neural crest induction and, thereby, link tight junctions to the control and timing of JNK signalling during early development. (
  • In metazoan adherens junctions, β-catenin links the cytoplasmic tail of classical cadherins to the F-actin-binding protein α-catenin. (
  • They accumulate at cell-cell contact sites and assemble into large macromolecular complexes named adherens junctions (AJs). (
  • The resulting cadherin-NPRAP-ABP/GRIP complexes serve as anchorages for AMPARs. (
  • Exogenous NPRAP that was bound to cadherins at adherens junctions of Madin-Darby canine kidney cells recruited ABP from the cytosol to form cadherin-NPRAP-ABP complexes, dependent on NPRAP interaction with the ABP PDZ domain 2. (
  • The cadherin-NPRAP-ABP complexes also bound GluR2. (
  • In cultured hippocampal neurons, dominant-negative mutants of NPRAP designed to disrupt tethering of ABP to NPRAP-cadherin complexes reduced surface levels of endogenous GluR2, indicating that interaction with cadherin-NPRAP-ABP complexes stabilized GluR2 at the neuronal plasma membrane. (
  • Because we find that NPRAP also binds to PSD-95, cadherin-NPRAP complexes may be linked to the PSD-95 scaffold, which is involved in tethering NMDAR and TARP-AMPAR complexes and which also interacts with neuroligins. (
  • The cadherin family is essential in maintaining the cell to cell contact between each other and regulating for cytoskeletal complexes. (
  • Cadherin/catenin complexes are hypothesized to play a role in the transduction of mechanical forces that shape cells and tissues during development, regeneration, and disease. (
  • In turn, these forces elicit mechanosensory signals from cadherin complexes that ultimately impact on cell phenotype and function in multiple cell types ( 29 , 30 ), including pancreatic islets ( 31 ). (
  • Further work analyzing the formation and stability of the E-cadherin-catenin complexes suggested that the E-cadherin- β -catenin complex was formed immediately after E-cadherin synthesis and was very stable. (
  • However, since γ -catenin was found to be only loosely associated with E-cadherin, it was determined that the main adhesive complexes consisted of E-cadherin, β -catenin, and α -catenin, although the existence of a separate E-cadherin- γ -catenin complex could not be ruled out [ 16 ]. (
  • The adherens junctions are composed of two major complexes: the nectin-based adhesions and cadherin-based adhesions. (
  • Like the nectins, the cadherin-based adhesions are highly integrated with other junctional complexes with some of the components of the cadherin adhesion complex binding to constituents of the nectin-based adhesions. (
  • E-Cadherin, however, was not detectable in these complexes. (
  • Neighboring cells are linked to each other by multimolecular complexes such as adherens junctions, desmosomes, and gap junctions. (
  • Our data suggest that in response to some agonists, both independent post-translational modifications contribute to the rapid induction of apoptosis by inhibiting the assembly of E-cadherin complexes on the plasma membrane. (
  • α-Catenin stabilises Cadherin-Catenin complexes and modulates actomyosin dynamics to allow pulsatile apical contraction. (
  • These complexes, which help regulate cell growth in addition to creating and maintaining epithelial layers, are known as adherens junctions and they typically include at least cadherin, β-catenin, and α-catenin. (
  • α-catenin participates in the formation and stabilization of adherens junctions by binding to β-catenin-cadherin complexes in the cell. (
  • δ-Catenin-1 (p120, p120ctn, cadherin-associated src substrate, 938 aa) is involved in cell-cell adhesion complexes together with E-*cadherin, α-, β-, and γ-catenins. (
  • Loss of E-cadherin is a defining characteristic of epithelial-mesenchymal transition (EMT), a process associated with tumour cell metastasis. (
  • We have previously demonstrated an EMT event during embryonic stem (ES) cell differentiation, and that loss of E-cadherin in these cells results in altered growth factor response and changes in cell surface localisation of promigratory molecules. (
  • We discuss the implication of loss of E-cadherin in ES cells within the context of cancer stem cells and current models of tumorigenesis. (
  • Our results confirm that loss of E-cadherin contributes to both mammary tumor initiation and metastasis, and establish a preclinical mouse model of human ILC that can be used for the development of novel intervention strategies to treat invasive breast cancer. (
  • Nonetheless, the molecular mechanisms that drive tumor development and progression upon loss of E-cadherin in breast cancer remain ill-defined. (
  • Conversely, acute loss of E-cadherin sensitizes cells to apoptosis by unknown post-translational mechanisms. (
  • In contrast, in vivo tissue specific knockout studies did not reveal a necessity of E-cadherin in the formation of intercellular junctions, raising the question if classical cadherins are necessary or if other classical cadherins can compensate for the loss of E-cadherin. (
  • Using primary keratinocytes as a model for de novo junction formation, it was found that loss of E-cadherin prevents the formation of a functional tight junctional barrier. (
  • Loss of E-cadherin in combination with knock down of the only other epidermal classical cadherin, P-cadherin, resulted in an almost complete loss of intercellular contacts showing that classical cadherins are crucial for desmosome formation. (
  • In this thesis it was found that loss of E-cadherin in primary keratinocytes is insufficient to enhance migration and proliferation, suggesting that in cancer cells E-cadherin interacts with other, E-cadherin independent pathways in the regulation of growth and migration. (
  • Binding of p-120 catenin and β {\displaystyle \beta } -catenin to the homodimer increases the stability of the classical cadherin. (
  • Both belong to the type I classical cadherin subfamily of vertebrates (which we henceforth refer to as simply cadherins unless necessary). (
  • The classical cadherin/catenin complex is the best understood intercellular adhesion complex and is found in most metazoan cohesive tissues ( 12 ). (
  • The classical cadherin cytoplasmic domain binds β-catenin, which in turn binds α-catenin. (
  • In addition to actin, the classical cadherin/γ-catenin (plakoglobin) complex can also associate with intermediate filaments in some instances ( 22 , 23 ). (
  • Of these, the classical cadherin family plays a central role, both during morphogenesis and in post-developmental tissue homeostasis. (
  • In addition, the question was asked if classical cadherin function is necessary for the formation of other intercellular contacts, such as desmosomes. (
  • Re-expression of either E- or P-cadherin can rescue not only desmosome formation but also tight junction function, showing that levels but not specific classical cadherin expression is crucial for the functional formation of intercellular junctions. (
  • In human umbilical vein endothelial cells (HUVECs), soluble IQGAP1 associated with VE-cadherin and the catenins, b, y, and a, but not N-cadherin. (
  • More VE-cadherin and less N-cadherin were associated with p120- and B -catenins in IQGAP1 knockdown cells. (
  • The increased interaction with the catenins, B and p120, possibly resulting from the decrease in N-cadherin, may explain the increase in VE-cadherin. (
  • Furthermore, this cleavage releases the cytoplasmic E‐cadherin to the cytosol and increases the levels of soluble β‐ and α‐catenins. (
  • In addition, we review the regulatory pathways controlling cadherin endocytosis and degradation, including regulation of cadherin endocytosis by catenins, cadherin ubiquitination, and growth factor receptor signaling pathways. (
  • Their main components are cadherins and catenins. (
  • Several types of catenins work with N-cadherins to play an important role in learning and memory (For full article, see Cadherin-catenin complex in learning and memory). (
  • Catenins play roles in cellular organization and polarity long before the development and incorporation of Wnt signaling pathways and cadherins. (
  • The intracellular functions of classical cadherins are mediated through the direct binding of two catenins: β-catenin and p120-catenin (also known as CTNND1 in vertebrates, and p120ctn in Drosophila). (
  • At maturity, sections of stromal equivalents were processed for Masson's trichrome or indirect immunofluorescence using antibodies against pan-, N-, or E-cadherins or α- or β-catenins. (
  • Western blots and indirect immunofluorescence revealed that, similarly to the native cornea, the epithelium reacted positively to antibodies against catenins (α and β) and E-cadherin. (
  • The endothelium of corneal constructs, whether of human or bovine origin, reacted mildly to catenins and N-cadherin. (
  • To this end, both partners develop a series of highly specific, morphologically well defined structures, i.e., tight junctions, cell-cell adherens junctions, and desmosomes ( Koch and Franke, 1994 ). (
  • Classical cadherins maintain the tone of tissues by forming a homodimer while desmosomes are the heterodimers. (
  • Desmosomal cadherins are responsible to maintain the function of desmosomes that is to overturn the mechanical stress of the tissues. (
  • As a component of both the adherens junctions and desmosomes, plakoglobin plays a pivotal role in the regulation of cell-cell adhesion. (
  • It was not until several years later that coimmunoprecipitation experiments showed that plakoglobin interacted with the desmosomal cadherin desmoglein, thereby confirming plakoglobin as a constituent of the desmosomes [ 13 ]. (
  • The main components of desmosomes are cadherins (desmogleins and desmocollins). (
  • Cell adhesion by adherens junctions and desmosomes relies on interactions between cadherin molecules. (
  • Finally, we show that Rab35 regulates myoblast fusion, a major cellular process under the control of cadherin-dependent signaling. (
  • Taken together, these results reveal that Rab35 regulates cadherin-dependent AJ formation and myoblast fusion. (
  • Chrifi I, Louzao-Martinez L, Brandt MM, van Dijk CGM, Bürgisser PE, Zhu C, Kros JM, Verhaar MC, Duncker DJ, Cheng C. CMTM4 regulates angiogenesis by promoting cell surface recycling of VE-cadherin to endothelial adherens junctions . (
  • Islet β-cell adhesion to recombinant Fc-cadherins emulates cell-cell interactions and positively regulates glucose-dependent insulin secretion. (
  • RAC1 regulates adherens junctions through endocytosis of E-cadherin. (
  • Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. (
  • Fbxo45 Binds SPRY Motifs in the Extracellular Domain of N-Cadherin and Regulates Neuron Migration during Brain Development. (
  • This finding that acetylation of nuclear E-cadherin regulates β-catenin activity expands our understanding of the acetylation of E-cadherin promotes colorectal cancer cell growth and suggests novel therapeutic approaches of targeting acetylation in tumors. (
  • Therefore, the aim of this thesis was to ask how E-cadherin regulates tight junctions and if E-cadherin has a specific function in the formation of tight junctions. (
  • Surprisingly, the basic assembly of tight junctions was not affected, suggesting that E-cadherin regulates a late step in the formation of a functional barrier. (
  • Cadherins are homophilic cell-cell adhesion molecules implicated in many fundamental processes, such as morphogenesis, cell growth, and differentiation. (
  • Cadherins are Ca 2+ -dependent homophilic synaptic CAMs that contribute to spine morphogenesis and synapse assembly and regulation (for review, see Takeichi and Abe, 2005 ). (
  • In general, classical cadherins exert their effect by homophilic interactions via their five characteristic extracellular (EC) repeats. (
  • E-cadherin contributes to the generation and maintenance of adherens junctions (AJ) via homophilic (E-cadherin-E-cadherin interaction) and, most often, homotypic (epithelial-epithelial cell interaction) cell adhesion (Figure 1 ). (
  • Diagrammatic representation of homophilic E-cadherin interaction and homotypic cell adhesion within the epithelium. (
  • Note that the exact mechanism of homophilic E-cadherin interaction is unclear. (
  • CD324 / E-cadherin is an epithelial cell surface molecule, which provides calcium-dependent homophilic interactions with E-cadherin of another cell. (
  • The extracellular domains of cadherins form Ca 2+ -dependent homophilic adhesions between neighboring cells. (
  • Cadherins promote cell adhesion via a homophilic mechanism as in the construction of tissues and of the whole animal body. (
  • Cadherins, which are members of a multigene family, mediate calcium-dependent homophilic cell-cell interactions through their N-terminal extracellular domain. (
  • Hypoglycosylated E-cadherin promotes the assembly of tight junctions through the recruitment of PP2A to adherens junctions. (
  • p120 catenin (p120ctn) binds to the cytoplasmic domain of cadherins in the juxtamembrane region, which has been implicated in regulating cell motility. (
  • p120 (sometimes called delta catenin) binds the juxtamembrane region of the cadherin. (
  • γ-catenin or gamma-catenin (plakoglobin) binds the catenin-binding region of the cadherin. (
  • B-catenin binds the cytoplasmic domain of some cadherins. (
  • β-Catenin (781 aa) binds E-cadherin and N-cadherin. (
  • Cadherin may acts as a negative regulator of signaling beta-catenin as it binds beta-catenin at the cell surface and thereby sequesters it from the nucleus. (
  • This gene encodes a member of the cadherin superfamily. (
  • This article focuses on adhesion receptors of the cadherin superfamily ( 19 , 20 ), which were referred to as uvomorulin in early work by Kemler et al. (
  • The fact that kidney development involves several morphogenetic processes (e.g., cell aggregation, cell movement, mesenchymal-epithelial conversion, cell sorting, and cell shape changes) that members of the classic cadherin superfamily of cell adhesion molecules have been implicated in validates studies of cadherin function during kidney organogenesis. (
  • Beyond the epithelium: cadherin function in fibrous connective tissues. (
  • The mammary epithelium is thought to be stabilized by cell-cell adhesion mediated mainly by E-cadherin (E-cad). (
  • Tumor invasion and metastasis are partly regulated by a switch from epithelial to mesenchymal cadherins in the transformed epithelium. (
  • We show that mammary-specific stochastic inactivation of conditional E-cadherin and p53 results in impaired mammary gland function during pregnancy through the induction of anoikis resistance of mammary epithelium, resulting in loss of epithelial organization and a dysfunctional mammary gland. (
  • Altogether, we show for the first time that the asymmetric localization of N-cadherin during mitosis indirectly influences fate segregation by differentially driving the allocation of progenitors to muscle versus dermal primordia, that the adhesive domain of N-cadherin maintains the integrity of the dermomyotome epithelium, which is necessary for myogenic specification, and that different molecular mechanisms underlie the establishment of pioneer and later myotomal waves. (
  • The host epithelium uses its epithelial junctions to form a tight but dynamic barrier with an external surface that is inhospitable to microbial attachment, secretes anti-microbial compounds, and has a rapid rate of self-renewal. (
  • One current model proposes that cells distinguish cadherin subtypes based on kinetic specificity rather than thermodynamic specificity, as different types of cadherin homotypic bonds have different lifetimes. (
  • However, knockdown or overexpression of neuronal N-cadherin does not influence the distribution of Par-3 or myelination, suggesting that homotypic interactions between SC and axonal N-cadherin are not essential for the events surrounding myelination. (
  • These focal adhesions are formed by homotypic interactions of cadherin molecules. (
  • N-Cadherin mediated homotypic aggregation among melanoma cells as well as heterotypic adhesion of melanoma cells to dermal fibroblasts and vascular endothelial cells. (
  • Emerging evidence indicates one factor that is key for this is the formation of homotypic cadherin mediated adherens junctions between β-cells. (
  • Thus, the PS1/γ‐secretase system stimulates disassembly of the E‐cadherin- catenin complex and increases the cytosolic pool of β‐catenin, a key regulator of the Wnt signaling pathway. (
  • We further demonstrated that CsA amplified epidermal growth factor (EGF)-stimulated EGF receptor (EGFR) tyrosine phosphorylation in JEG-3 cells, and inhibition of EGFR tyrosine phosphorylation by AG1478, an EGFR tyrosine kinase inhibitor, abolished the down-regulation of E-cadherin by CsA through ERK signaling pathway. (
  • The E-cadherin/β-catenin signaling pathway plays a critical role in the maintenance of epithelial architecture and regulation of tumor progression. (
  • Tyrosine phosphorylation of vascular endothelial cadherin (VE-cad) leads to the disruption of endothelial adherens junctions and increases the transendothelial migration (TEM) of leukocytes. (
  • Our findings show that the high-concentration glucose-induced disruption of endothelial adherens junctions is mediated by tyrosine phosphorylation of VE-cad through PKC-β and MLC phosphorylation. (
  • We previously reported that anthrax lethal toxin (LT) induces human endothelial barrier dysfunction in a cell death-independent manner with actin stress fiber formation and disruption of adherens junctions (AJs). (
  • Disruption of adherens junctions promotes tumor cell invasion and metastasis 6 . (
  • Moreover, Pkp3 forms a complex with Rap1 GTPase, promoting its activation and facilitating desmosome assembly.We show further that Pkp3 deficiency causes disruption of an E-cadherin/Rap1 complex required for adherens junction sealing.These findings reveal Pkp3 as a coordinator of desmosome and adherens junction assembly and maturation through its functional association with Rap1. (
  • IFN-γ increases permeability of intestinal vessels by disruption of VE-cadherin junctions, associated with increased inflammation and progression of IBD. (
  • Imatinib inhibits VE-cadherin disruption, reduces vascular permeability, and ameliorates the course of the disease. (
  • Fluorescent imaging of junctions formed from wild-type and mutant E-cadherins in cultured cells confirm conclusions derived from structural evidence. (
  • Here we identify the small GTPase Rab35 as a new regulator of cadherin trafficking and stabilization at cell-cell contacts in C2C12 myoblasts and HeLa cells. (
  • VE-cad tyrosine phosphorylation, adherens junction integrity and TEM of monocytes in human umbilical vein endothelial cells (HUVECs) treated with high-concentration glucose were evaluated. (
  • E-N-cadherin heterodimers define novel adherens junctions connecting endoderm-derived cells. (
  • In this paper, we show that this "cadherin switch" hypothesis does not hold for diverse endoderm-derived cells and cells of tumors derived from them. (
  • We show that the cadherins in a major portion of AJs in these cells can be chemically cross-linked in E-N heterodimers. (
  • We also show that cells possessing E-N heterodimer AJs can form semistable hemihomotypic AJs with purely N-cadherin-based AJs of mesenchymally derived cells, including stroma cells. (
  • By acting as a dynamic link between adjacent cells in a monolayer, adherens junctions (AJs) maintain the integrity of epithelial tissues while allowing for neighbor exchange. (
  • The expression of VE-cadherin in breast cancer cells modulates cell dynamics as a function of tumor differentiation and promotes tumor-endothelial cell interactions. (
  • It was found that the levels of integrin alpha1 and VE-cadherin mRNA increased during co-culturing of activated endothelium cells with mesenchymal stromal cells. (
  • We showed that CsA down-regulated E-cadherin transcription and translation in human primary cultured trophoblast cells and choriocarcinoma cell line JEG-3. (
  • Immunofluorescent images of E-cadherin in control and PP6c KD cells with or without IC261 treatment. (
  • (E) An immunoblot of PP6c, PP2Ac, E-cadherin and actin in cells with PP6c knockdown compared to control. (
  • Cadherins (named for "calcium-dependent adhesion") are a type of cell adhesion molecule (CAM) that are important in the formation of adherens junctions to bind cells with each other. (
  • Although classical cadherins take a role in cell layer formation and structure formation, desmosomal cadherins focus on resisting the catastrophe towards the cells. (
  • It has been observed that cells containing a specific cadherin subtype tend to cluster together to the exclusion of other types, both in cell culture and during development. (
  • For example, cells containing N-cadherin tend to cluster with other N-cadherin-expressing cells. (
  • The homodimeric cadherins create cell-cell adhesion with cadherins present in the membranes of other cells through changing conformation from cis-dimers to trans-dimers. (
  • Using their most membrane-distal EC1 repeat, cadherin protomers on opposed cells swap strands with each other to form adhesive dimers. (
  • In addition, mechanical stimulation of cells through the extracellular domain of cadherins results in vinculin-dependent cell stiffening ( 25 ), and membrane protrusion reorientation via a mechanism involving γ-catenin and intermediate filaments ( 26 ). (
  • We have previously conducted a genome-wide siRNA screen and a 4000 compound 'known drug' screen in isogenic breast MCF10A cells with and without E-cadherin expression to identify vulnerabilities in the MCF10A- CDH1 −/− cells that could be exploited in an SL manner [ 7 ]. (
  • The present study was carried out to investigate the functional significance of N-cadherin in melanoma cells. (
  • Blocking of N-cadherin-mediated intercellular interaction by N-cadherin-specific antibodies increased the number of cells undergoing apoptosis. (
  • Furthermore, N-cadherin promoted migration of melanocytic cells over dermal fibroblasts, suggesting that N-cadherin may also play a role in metastasis. (
  • Together, these results indicate that the cadherin subtype switching from E- to N-cadherin during melanoma development not only frees melanocytic cells from the control by keratinocytes but also provides growth and possibly metastatic advantages to melanoma cells. (
  • In normal human skin, E-cadherin is expressed on the cell surface of keratinocytes and melanocytes and is the major adhesion molecule between epidermal melanocytes and keratinocytes (6 , 7 , 8) , whereas N-cadherin is expressed by fibroblasts and endothelial cells. (
  • 2. Hemidesmosomes Communicating (gap) junctions THANKS for your attention :) Prof. Dr. Wael Abu Zaid Prof. Dr. Mohamed Zayed Prof. Dr. Nehad Samir Specialized junctions form when cells come into contact with one another and with the extracellular matrix at specific sites on the contacting cell membranes. (
  • We propose that aberrant E-cadherin expression is a critical contributing factor to neoplasia and the early stages of tumorigenesis in the absence of EMT by altering growth factor response of the cells, resulting in increased proliferation, decreased apoptosis, and acquisition of a stem cell-like phenotype. (
  • This structure is likely to involve E-cadherin cis-homodimers binding similar cis-homodimers on adjacent cells to form transhomodimers, although the exact mechanism of this interaction is unclear [ 3 ]. (
  • E-cadherin cis-dimers form transhomodimers with E-cadherin molecules on neighbouring cells to facilitate epithelial integrity. (
  • A similar cell junction in non-epithelial, non-endothelial cells is the fascia adherens. (
  • Adherens junctions were, for many years, thought to share the characteristic of anchor cells through their cytoplasmic actin filaments. (
  • 1 ) reported that human islet cells contain specialized membrane domains that are compatible with the ultrastructural features of two types of intercellular junctions: tight junctions and gap junctions. (
  • As a result, cells that are in contact with each other through cadherin-mediated junctions sense tension forces that are directly proportional to the degree of actin-anchored cadherin adhesions. (
  • This approach allowed them to emulate cadherin-mediated adhesions in single β-cells adherent to a substrate that presented high concentrations of recombinant E-cad/Fc, N-cad/Fc, or P-cad/Fc as if presented by another cell ( Fig. 1 ). (
  • Cell junctions regulate small-molecule trafficking between cells, the organization of cells into tissues, and the adherence of cells to each other and the extracellular matrix. (
  • Gap junctions are clusters of tightly packed channels that allow small molecules (metabolites, second messengers, and ions) to travel between adjoining cells 1 . (
  • This assembly of cell-cell junctions is highly coordinated both spatially and functionally, with the adhesions between cells forming first and the barrier forming second. (
  • N-cadherin is expressed in neuronal and fibroblastic cells, while VE-cadherin is expressed in endothelial cells. (
  • Local gene missexpression confirms that N-cadherin-mediated adhesion is sufficient to promote myotome colonization, whereas its absence drives cells towards the subectodermal domain, hence coupling the asymmetric distribution of N-cadherin to a shift in mitotic orientation and to fate segregation. (
  • Morphological analysis of nephrogenesis in R-cadherin −/− mice in vivo and in vitro revealed defects in the development of both ureteric bud-derived cells and metanephric mesenchyme-derived cells. (
  • After treatment of breast cancer cells with drugs, we found that two independent modifications of E-cadherin inhibit its cell surface transport. (
  • and ubiquitylation ( D'Souza-Schorey, 2005 ) control the trafficking and assembly of E-cadherin in mammalian cells. (
  • Caco-2 cells labeled for tight junction molecule cingulin (green), actin (red), vinculin (pink) and DNA (blue). (
  • Dual Role of E-cadherin in the regulation of invasive collective migration of mammary carcinoma cells. (
  • They are important in the formation of ADHERENS JUNCTIONS between cells. (
  • For instance, when an epithelial layer is complete and the adherens junctions indicate that the cell is surrounded, β-catenin may play a role in telling the cell to stop proliferating, as there is no room for more cells in the area. (
  • F9 embryonal carcinoma cells are similar to the P19 cells shown in Figure 1 and normally have cell-to-cell adhesion mediated by E-cadherin with β-catenin bound to the cytoplasmic domain of E-cadherin. (
  • F9 cells were genetically engineered to lack β-catenin, resulting in increased association of plakoglobin with E-cadherin. (
  • In F9 cells lacking both β-catenin and plakoglobin, very little E-cadherin and α-catenin accumulated at the cell surface. (
  • Cells are linked together dynamically by adhesion molecules, such as the classical cadherins. (
  • 2 Increasingly, we are coming to realize that the impact of cadherin-actin cooperation also reflects how adhesion couples the contractile actin cytoskeletons of cells together. (
  • Figure: Intracellular adherens junctions are initiated by interactions between extracellular domains of membrane-bound cadherins (shown in blue) on adjacent cells. (
  • By forging these robust links, cadherin adhesions not only connect neighbouring cells but allow cells to coordinate their movements, maintain tissue integrity, and relay a myriad of signals important for proper tissue functions. (
  • In epithelial tissues, cells are joined by extensive cell contacts or junctions, and HSV and other herpesviruses spread across these cell junctions. (
  • In some hearts, graft cells formed adherens and gap junctions with host cardiomyocytes, suggesting electromechanical coupling. (
  • In contrast, Connold et al 5 reported that embryonic rat cardiomyocytes formed organized gap junctions with other graft cells when grafted into injured rat hearts, suggesting that some differentiation could occur. (
  • 4) Will grafted cells integrate, ie, form electrical and mechanical junctions, with host cardiomyocytes? (
  • VE-cadherin is the major component of endothelial adherens junctions and is specific to endothelial cells. (
  • Non-junctional E-cadherin clusters regulate the actomyosin cortex in the C. (
  • Substrate stiffness and VE-cadherin mechano-transduction coordinate to regulate endothelial monolayer integrity. (
  • Cadherins are cell adhesion molecules that regulate numerous adhesive interactions during embryonic development and adult life. (
  • Here, we review the evidence for this and discuss the mechanisms by which these adherens junctions might regulate insulin vesicle trafficking as well as the implications this has for understanding the dysregulation of insulin secretion seen in pathogenic states. (
  • Tight junctions are barriers that regulate the paracellular movement of solutes down their electro-osmotic gradients. (
  • The distinct expression of R-cadherin in the induced aggregating metanephric mesenchyme suggests that it may regulate the mesenchymal-epithelial transition during kidney development. (
  • This selective permeable barrier is achieved by intercellular tight junction (TJ) structures, which regulate paracellular permeability. (
  • 2001. Platelet/endothelial cell adhesion molecule-1 and VE-cadherin / ß-catenin cooperatively regulate FGF-induced modulations of adherens junction functions. (
  • One pathway through which E-cadherin may regulate the functional barrier is by controlling expression levels of the barrier promoting claudin 14. (
  • Adherens junctions, which play a central role in intercellular adhesion, comprise clusters of type I classical cadherins that bind via extracellular domains extended from opposing cell surfaces. (
  • Adherens junctions are important mediators of intercellular adhesion, but they are not static structures. (
  • Thus, endocytosis, degradation, and recycling of cadherins are crucial for dynamic regulation of adherens junctions and control of intercellular adhesion. (
  • Classical cadherins mediate Ca2+-dependent intercellular adhesion and are essential for tissue morphogenesis and maintenance. (
  • The integrity of the cadherin-catenin complex is negatively regulated by phosphorylation of beta-catenin by receptor tyrosine kinases (RTKs) and cytoplasmic tyrosine kinases (Fer, Fyn, Yes, and Src), which leads to dissociation of the cadherin-catenin complex. (
  • In all three ectodomain crystals, cadherins dimerize through a trans adhesive interface and are connected by a second, cis, interface. (
  • Trans cadherin interactions result in an adhesive dimer interface between the interacting EC1 domains. (
  • N-glycosylation affects the adhesive function of E-Cadherin through modifying the composition of adherens junctions (AJs) in human breast carcinoma cell line MDA-MB-435. (
  • Although there is some controversy surrounding the precise function of distinct regions of E-cadherin in cell-cell adhesion, many studies have shown the HAV domain, located on residues 79-81 of the EC1 domain, to play a key role in its adhesive function by forming a hydrophobic pocket into which a Tryptophan residue 2 (Trp2) from an adjacent E-cadherin molecule can dock. (
  • This flexibility suggests a novel mechanism for generating both cis and trans interactions and for propagating these adhesive interactions along the junction. (
  • Constitutively phosphorylated E-cadherin (S846D) is unable to localize at cell-cell contacts and has decreased adhesive activity. (
  • However, a structural basis for cadherin association with AMPA receptors is not known. (
  • Cadherins are calcium-dependent adhesion molecules responsible for the establishment of tight cell-cell contacts. (
  • There are multiple classes of cadherin molecules, each designated with a prefix (in general, noting the types of tissue with which it is associated). (
  • Among the molecules involved in the intercellular communication are cadherins, which have been shown to play a critical role in tumor formation and progression. (
  • The cadherin family is divided into classical (Type I) and nonclassical (Type II) subtypes, as well as other categories which include protocadherins and cadherin-related molecules. (
  • Mutations of Trp2 and the alanine residue of the HAV domain, W2A and A80I, respectively, have been shown to abolish trans- but not cis-homodimerisation of E-cadherin molecules, thus demonstrating the key roles of these amino acids in the formation of E-cadherin mediated cell-cell contact [ 2 ]. (
  • 21 ). Over the past three decades, the function of cadherins in epithelia has evolved from simple cell-cell adhesion molecules that populate subcellular domains called "adherens junctions" to biochemical transducers of signaling processes that contribute to the development, homeostasis, and function of multiple tissues ( 22 - 24 ). (
  • The main components of tight junctions are claudins, occludins, and junctional adhesion molecules (JAMs). (
  • The resulting three-dimensional maps reveal individual cadherin molecules forming discrete groups and interacting through their tips. (
  • Two of these, the adherens junction and the desmosome, contain cadherin cell adhesion molecules. (
  • Proteolysis was selective, since important components of adherens junctions (E-cadherin) or signaling molecules (extracellular signal-regulated kinases ERK1/2) were not degraded. (
  • At AJs, E-cadherin serves as an essential cell adhesion molecules (CAMs). (
  • Cell-cell adherens junctions (AJs), the most common type of intercellular adhesions, are important for maintaining tissue architecture and cell polarity and can limit cell movement and proliferation. (
  • Knockdown of Rab35 or expression of a dominant-negative form of Rab35 impaired N- and M-cadherin recruitment to cell-cell contacts, their stabilization at the plasma membrane, and association with p120 catenin and led to their accumulation in transferrin-, clathrin-, and AP-2-positive intracellular vesicles. (
  • Whereas β-catenin is crucial for cadherin function, the role of p120-catenin is less clear and appears to vary between organisms. (
  • This study shows that p120-catenin has a conserved role in regulating the endocytosis of cadherins, but that its ancestral role might have been to promote endocytosis, followed by the acquisition of a new inhibitory role in vertebrates. (
  • In Drosophila, p120-catenin facilitates endocytosis of the dynamic E-cadherin-Bazooka subcomplex, which is followed by its recycling. (
  • A role for the adherens junction regulator P120-Catenin in retinal patterning was establised through its regulation of normal adherens junction integrity. (
  • Based upon live visualization of the P120-Catenin mutant as well as genetic data, it is concluded that P120-Catenin is acting to stabilize E-cadherin and adherens junction integrity during eye development (Larson, 2008). (
  • They are key components of adherens junctions (AJs). (
  • They are regularly formed, broken, and rearranged in a variety of situations, requiring changes in the amount of cadherins, the main adhesion molecule in adherens junctions, present at the cell surface. (
  • The mouse monoclonal antibody 67A4 recognizes CD324 / E-cadherin, an approximately 100 kDa epithelial cell adhesion molecule, whose detection is important for determination of invasive potential of epithelial neoplasms. (
  • The cadherin 5 molecule may play a role in the permeability properties of vascular endothelium. (
  • Lastly, we discuss the proteolytic cleavage of cadherins at the plasma membrane. (
  • Further investigation using this system resulted in a model whereby cadherins are constantly and spontaneously recruited to the plasma membrane , form lateral catenin-dependent associations and are subsequently released from these clusters in an active, ATP-dependent manner. (
  • E-cadherin loss leads to disturbances in receptor signalling and plasma membrane trafficking and organisation, creating druggable vulnerabilities. (
  • Specifically, we find that myosin, E-cadherin, Echinoid, the plasma membrane, microtubules and the Cdc42 small GTPase respond dynamically during wound repair. (
  • Consequently, E-cadherin trafficking to the plasma membrane was inhibited. (
  • Loss of plasma membrane localization of E-cadherin accelerates the induction of apoptosis, because prevention of O-GlcNAcylation by deletion mutagenesis restored PIPKIγ binding, E-cadherin trafficking, and attenuated apoptosis. (
  • We conclude that these heterodimers are the major AJ constituents of several endoderm-derived tissues and tumors and that the prevailing concept of antagonistic roles of these two cadherins in developmental and tumor biology has to be reconsidered. (
  • To generate a good preclinical model of invasive breast cancer, we have taken a tissue-specific approach to somatically inactivate p53 and E-cadherin, the cardinal cell-cell adhesion receptor that is strongly associated with tumor invasiveness. (
  • Acetylation of nuclear E-cadherin attenuated its interaction with β-catenin, which therefore released β-catenin from the complex, resulting in increased expression of its downstream genes and accelerated tumor growth and migration. (
  • Taken together, our findings reveal a novel mechanism of tumor progression through posttranslational modification of E-cadherin, which may serve as a potential drug target of tumor therapy. (
  • E-cadherin is a tumor suppressor and found to be down regulated in many tumors. (
  • Plakophilin 3 mediates Rap1-dependent desmosome assembly and adherens junction maturation. (
  • Immunofluorescence and immunoelectron microscopic studies revealed that p205 was concentrated at cadherin-based cell-to-cell AJ of various tissues. (
  • Later in life, cadherins are responsible for the homeostasis of many tissues. (
  • Insulin receptor substrate 1 (IRS1) was overexpressed in ECs using the VE-cadherin promoter to create ECIRS1 TG mice, which elevated pAkt activation and expressions of vascular endothelial growth factor (VEGF), Flk1, and VE-cadherin in ECs and granulation tissues (GTs) of full-thickness wounds. (
  • Mice lacking plakoglobin have cell adhesion defects in many tissues, although β-catenin substitutes for plakoglobin at many cellular junctions. (
  • Other classical cadherins such as N-, P-, or VE isotypes are found in neural, placental, or vascular endothelial tissues. (
  • Chlamydia pneumoniae infection promotes monocyte transendothelial migration by increasing vascular endothelial cell permeability via the tyrosine phosphorylation of VE-cadherin. (
  • Increased serum soluble vascular endothelial cadherin levels in patients with chronic spontaneous urticaria. (
  • The concentration of activated pMyosin II at these punctate adherens junctions suggests that these glial bands are under tension, forming a physical barrier between cone columns and contributing to mechanical stress anisotropies in the epithelial sheet. (
  • Using a knockdown and substitution system, we studied whether ZO-1 binding to α-catenin is required for coupling tight junction assembly to the formation of adherens junctions. (
  • T-cadherin gene variants are associated with nephropathy in subjects with type 1 diabetes. (
  • The single nucleotide polymorphisms (SNPs) rs12596316AG genotype of the T-cadherin (CDH13) gene is associated with the susceptibility to metabolic syndrome (MS) among ethnic Han Chinese. (
  • To further investigate the role of N-cadherin, mice displaying SC-specific gene ablation of N-cadherin were generated and characterized. (
  • To determine whether β-catenin mediates compensation on N-cadherin deletion, SC-specific gene ablation of β-catenin was generated and characterized. (
  • The E-cadherin gene ( CDH1 ) is frequently mutated in diffuse gastric cancer and lobular breast cancer, and germline mutations predispose to the cancer syndrome Hereditary Diffuse Gastric Cancer. (
  • In addition, gene delivery was enhanced significantly under culture conditions that disrupted adherens junctions (AJ) but decreased upon AJ formation. (
  • Using a doxycycline regulatable system we showed that expression of dominant negative E-cadherin enhanced gene transfer in a dose-dependent manner. (
  • This was accompanied by the restoration of VE-cadherin expression and membrane localization, and attenuation of the LT-induced increase in monolayer permeability to albumin. (
  • Localization of endogenous E-cadherin in response to PP6c knockdown and casein kinase 1 inhibition. (
  • Knockdown of N-cadherin in SCs cocultured with DRG neurons disrupts Par-3 localization and delays the initiation of myelination. (
  • We set out to characterize and manipulate the expression and localization of N-cadherin in both SCs and DRG neurons in an in vitro coculture system, and find that N-cadherin, β-catenin, and Par-3 colocalize at the SC-axon interface and that asymmetric localization is induced on contact. (
  • Knockdown of N-cadherin in SCs disrupts Par-3 localization and delays the initiation of myelination. (
  • Although the nuclear localization of E-cadherin has been frequently observed in various types of cancers, little is known regarding the functional consequences of its nuclear translocation. (
  • Gap and adherens junctions formed between neonatal and adult cardiomyocytes in coculture, as evidenced by dye transfer and localization of cadherin and connexin43 at intercellular junctions. (
  • E-cadherin (E-cad) down-regulation in epithelial carcinomas is associated with malignant progression ( 1 - 6 ). (
  • Written and edited by experts in the field, this collection from Cold Spring Harbor Perspectives in Biology reviews our understanding of the organization, regulation, and dynamics of cell-cell junctions and the roles they play in morphogenesis, tissue homeostasis, and disease. (
  • The modifications of E-cadherin by O-GlcNAcylation and lack of pro-region processing represent novel mechanisms for rapid regulation of cell surface transport of E-cadherin in response to intoxication. (
  • Dies führte zur Frage, ob E-cadherin für die Bildung epidermaler Desmosomen entbehrlich ist und wie die spezifische Regulation von epidermalen zonula occludens stattfindet. (
  • Neben der Regulation von Zelladhäsion spielt E-cadherin eine wichtige Rolle bei der Regulation anderer zellulärer Prozesse wie Proliferation und Migration. (
  • A major feature is the generation of contractile forces at junctions, yielding patterns of tension that contribute to tissue integrity and patterning. (
  • We show that a molecular layer seen in crystal structures of E- and N-cadherin ectodomains reported here and in a previous C-cadherin structure corresponds to the extracellular architecture of adherens junctions. (
  • Prior to dermomyotome dissociation into dermis and muscle progenitors, when mitoses become perpendicularly oriented, N-cadherin remains associated only with the apical cell located in apposition to the myotome, generating molecular asymmetry between basal and apical progeny. (
  • These data indicate that CK1 is a novel negative regulator of cadherin-based cell-cell contacts. (
  • Diese Arbeit zeigt das E-cadherin kein direkter Regulator der Keratinozyten Proliferation und Migration ist. (
  • In this chapter, we review the involvement of cadherin endocytosis in development and disease. (
  • This was confirmed in endocytosis assays, which revealed a requirement for Cdc42, Arp2/3, and Dynamin for normal rates of E-cadherin internalization. (
  • We show that the major CK1 phosphorylation site of E-cadherin is serine 846, a highly conserved residue between classical cadherins. (
  • Therefore, the cadherin/catenin/actin linkage may be highly dynamic, or its components may require a specific conformation not recapitulated in vitro to bind actin. (
  • CK1 colocalizes with E-cadherin and phosphorylates the cytoplasmic domain of E-cadherin in vitro and in a cell culture system. (
  • In vitro studies have suggested that N-cadherin plays a role in myogenesis, but its role in vivo remains poorly understood. (
  • Second, during in vitro studies of mesenchymal-epithelial conversion, significantly fewer epithelial structures developed from R-cadherin −/− kidneys than from wild-type kidneys. (
  • What is the role of non-junctional E-cadherin clusters? (
  • Non-junctional E-cadherin clusters play a non-canonical role in stabilizing the cortex and resisting its flow, in addition to their well-characterized role in mediating cell-cell junctions. (
  • Molecularly, E-cadherin localizes and tunes EGFR activity and junctional tension to inhibit premature TJ complex formation in lower layers while promoting increased tension and TJ stability in the granular layer 2. (
  • In conclusion, our data identify an E-cadherin-dependent mechanical circuit that integrates adhesion, contractile forces and biochemical signaling to drive the polarized organization of junctional tension necessary to build an in vivo epithelial barrier. (
  • f Quantification of whole-mount junctional intensities of E-cadherin, ZO-1, and vinculin in different epidermal layers. (
  • Using quantitative whole-mount imaging, genetic ablation, and traction force microscopy and atomic force microscopy, we find that ubiquitously localized E-cadherin coordinates tissue polarization of tension-bearing adherens junction (AJ) and F-actin organization to allow formation of an apical TJ network only in the uppermost viable layer. (
  • g SG2 projections from apical to subapical cell-cell junctions stained for vinculin, E-cadherin, and ZO-1 showing an basolateral AJs network and an apical TJ network. (
  • between columns, N-cadherin-mediated adherens junctions stabilize Müller glial apical processes. (
  • They can appear as bands encircling the cell (zonula adherens) or as spots of attachment to the extracellular matrix (adhesion plaques). (
  • Klassische Cadherine sind Calcium abhängige Zelladhäsionsmoleküle und ein wichtiger Bestandteil der zonula adherens. (
  • Dabei hing nicht nur die Bildung von zonula adherens, sondern auch die von Desmosomen und zonula occludens von der funktionalen Aktivität von E-cadherin ab. (
  • Nur die Barriere Funktion der zonula occludens im stratum granulosum der Epidermis war nach genetischer Inaktivierung von E-cadherin beeinträchtigt. (
  • Obwohl zonula occludens in Abwesenheit von E-cadherin strukturell vorhanden sind, konnte gezeigt werden dass diese Strukturen keine funktionelle Barriere bilden. (
  • Die klassischen Cadherine E- und P-Cadherin zeigen funktionelle Redundanz bei sowohl Desmosomenbildung als auch bei der Bildung einer funktionalen zonula occludens barriere. (
  • Generation of a barrier in multi-layered epithelia like the epidermis requires restricted positioning of functional tight junctions (TJ) to the most suprabasal viable layer. (
  • True or False: Tight junctions form BEFORE adherens junctions. (
  • Soon after the adherens junctions begin to form, the tight junctions assemble. (
  • Another critical component of the tight junctions is ZO-1. (
  • While the individual components of the adherens and tight junctions have emerged, an appreciation of how these components are coupled to give rise to a coordinated assembly process is not understood. (
  • how are tight junctions formed? (
  • Tsukita S, Furuse M, Itoh M (2001) Multifunctional strands in tight junctions. (
  • Expression of gE-gI without other HSV polypeptides did not cause redistribution of either ZO-1 or β-catenin or alter tight-junction functions. (
  • By spreading rapidly from cell to cell through a space that is isolated by tight junctions, HSV races against the mounting immune response and also avoids neutralization by anti-HSV antibodies. (
  • b Newborn epidermal whole-mount immunofluorescence analysis for tension-high (vinculin) adherens junctions (E-cadherin). (
  • Note that vinculin-positive junctions are primarily present in the granular layer 2 (SG2). (
  • Vinculin is associated with the E-cadherin adhesion complex. (
  • however, it is likely that α-catenin acts in concert with vinculin to bind to actin and help stabilize the junctions. (
  • In a nutshell, vinculin could serve as a bridge to link between the cadherin and actin layers. (
  • Our research aims to understand the 3-dimensional architecture and dynamics of these junctions. (
  • Here we discuss recent developments in understanding how cadherin junctions integrate signaling and cytoskeletal dynamics to sense and generate force. (
  • Baum B, Georgiou M (2011) Dynamics of adherens junctions in epithelial establishment, maintenance, and remodeling. (
  • Cadherin-based cell-cell adhesions are dynamically established and/or disrupted during various physiological and pathological processes. (
  • Deletions in the cytoplasmic domain of E-Cadherin which eliminate catenin binding also result in a loss of cell adhesion, indicating that this binding is essential for E-Cadherin function. (
  • The authors also discuss the roles of cell-cell junctions in specific developmental and physiological processes, such as hearing, skeletal myogenesis, and neural circuit assembly, as well as in diseases such as cancer. (
  • Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for neural, and P- for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). (
  • Invitrogen antibodies include antibodies to study all five types of cell junctions, exclusive ABfinity rabbit recombinant monoclonal antibodies, and antibody-labeled conjugates to visualize a broad target range, with high specificity. (