Specialized regions of the cell membrane composed of pits coated with a bristle covering made of the protein CLATHRIN. These pits are the entry route for macromolecules bound by cell surface receptors. The pits are then internalized into the cytoplasm to form the COATED VESICLES.
Vesicles formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles are covered with a lattice-like network of coat proteins, such as CLATHRIN, coat protein complex proteins, or CAVEOLINS.
The main structural coat protein of COATED VESICLES which play a key role in the intracellular transport between membranous organelles. Each molecule of clathrin consists of three light chains (CLATHRIN LIGHT CHAINS) and three heavy chains (CLATHRIN HEAVY CHAINS) that form a structure called a triskelion. Clathrin also interacts with cytoskeletal proteins.
Membrane-bound compartments which contain transmitter molecules. Synaptic vesicles are concentrated at presynaptic terminals. They actively sequester transmitter molecules from the cytoplasm. In at least some synapses, transmitter release occurs by fusion of these vesicles with the presynaptic membrane, followed by exocytosis of their contents.
Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.
An organization of cells into an organ-like structure. Organoids can be generated in culture. They are also found in certain neoplasms.
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.
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.
Vesicles that are involved in shuttling cargo from the interior of the cell to the cell surface, from the cell surface to the interior, across the cell or around the cell to various locations.
A stack of flattened vesicles that functions in posttranslational processing and sorting of proteins, receiving them from the rough ENDOPLASMIC RETICULUM and directing them to secretory vesicles, LYSOSOMES, or the CELL MEMBRANE. The movement of proteins takes place by transfer vesicles that bud off from the rough endoplasmic reticulum or Golgi apparatus and fuse with the Golgi, lysosomes or cell membrane. (From Glick, Glossary of Biochemistry and Molecular Biology, 1990)
A 700-kDa cytosolic protein complex consisting of seven equimolar subunits (alpha, beta, beta', gamma, delta, epsilon and zeta). COATOMER PROTEIN and ADP-RIBOSYLATION FACTOR 1 are principle components of COAT PROTEIN COMPLEX I and are involved in vesicle transport between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.
Membrane-limited structures derived from the plasma membrane or various intracellular membranes which function in storage, transport or metabolism.
TRANSPORT VESICLES formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles is covered with a lattice-like network of COP (coat protein complex) proteins, either COPI or COPII. COPI coated vesicles transport backwards from the cisternae of the GOLGI APPARATUS to the rough endoplasmic reticulum (ENDOPLASMIC RETICULUM, ROUGH), while COPII coated vesicles transport forward from the rough endoplasmic reticulum to the Golgi apparatus.
A saclike, glandular diverticulum on each ductus deferens in male vertebrates. It is united with the excretory duct and serves for temporary storage of semen. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found.
Techniques to partition various components of the cell into SUBCELLULAR FRACTIONS.
Vesicles formed when cell-membrane coated pits (COATED PITS, CELL-MEMBRANE) invaginate and pinch off. The outer surface of these vesicles is covered with a lattice-like network of the protein CLATHRIN. Shortly after formation, however, the clathrin coat is removed and the vesicles are referred to as ENDOSOMES.
Vesicles derived from the GOLGI APPARATUS containing material to be released at the cell surface.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
A family of large adaptin protein subunits of approximately 100 kDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 2.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
The part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.
Condensed areas of cellular material that may be bounded by a membrane.
Thin structures that encapsulate subcellular structures or ORGANELLES in EUKARYOTIC CELLS. They include a variety of membranes associated with the CELL NUCLEUS; the MITOCHONDRIA; the GOLGI APPARATUS; the ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.
A subclass of clathrin assembly proteins that occur as monomers.
A receptor that is specific for IGF-II and mannose-6-phosphate. The receptor is a 250-kDa single chain polypeptide which is unrelated in structure to the type 1 IGF receptor (RECEPTOR, IGF TYPE 1) and does not have a tyrosine kinase domain.
A family of large adaptin protein subunits of approximately 90 KDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 1.
A protein complex comprised of COATOMER PROTEIN and ADP RIBOSYLATION FACTOR 1. It is involved in transport of vesicles between the ENDOPLASMIC RETICULUM and the GOLGI APPARATUS.
An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE.
The sum of the weight of all the atoms in a molecule.
A bile salt formed in the liver by conjugation of deoxycholate with taurine, usually as the sodium salt. It is used as a cholagogue and choleretic, also industrially as a fat emulsifier.
Cellular release of material within membrane-limited vesicles by fusion of the vesicles with the CELL MEMBRANE.
The movement of materials (including biochemical substances and drugs) through a biological system at the cellular level. The transport can be across cell membranes and epithelial layers. It also can occur within intracellular compartments and extracellular compartments.
A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.
A family of high molecular weight GTP phosphohydrolases that play a direct role in vesicle transport. They associate with microtubule bundles (MICROTUBULES) and are believed to produce mechanical force via a process linked to GTP hydrolysis. This enzyme was formerly listed as EC 3.6.1.50.
Artificial, single or multilaminar vesicles (made from lecithins or other lipids) that are used for the delivery of a variety of biological molecules or molecular complexes to cells, for example, drug delivery and gene transfer. They are also used to study membranes and membrane proteins.
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.
A constitutively expressed subfamily of the HSP70 heat-shock proteins. They preferentially bind and release hydrophobic peptides by an ATP-dependent process and are involved in post-translational PROTEIN TRANSLOCATION.
Specific particles of membrane-bound organized living substances present in eukaryotic cells, such as the MITOCHONDRIA; the GOLGI APPARATUS; ENDOPLASMIC RETICULUM; LYSOSOMES; PLASTIDS; and VACUOLES.
An iron-binding beta1-globulin that is synthesized in the LIVER and secreted into the blood. It plays a central role in the transport of IRON throughout the circulation. A variety of transferrin isoforms exist in humans, including some that are considered markers for specific disease states.
The rate dynamics in chemical or physical systems.
A class of morphologically heterogeneous cytoplasmic particles in animal and plant tissues characterized by their content of hydrolytic enzymes and the structure-linked latency of these enzymes. The intracellular functions of lysosomes depend on their lytic potential. The single unit membrane of the lysosome acts as a barrier between the enzymes enclosed in the lysosome and the external substrate. The activity of the enzymes contained in lysosomes is limited or nil unless the vesicle in which they are enclosed is ruptured. Such rupture is supposed to be under metabolic (hormonal) control. (From Rieger et al., Glossary of Genetics: Classical and Molecular, 5th ed)
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 family of large adaptin protein complex subunits of approximately 90-130 kDa in size.
Any spaces or cavities within a cell. They may function in digestion, storage, secretion, or excretion.
A family of medium adaptin protein subunits of approximately 45 KDa in size. They have been primarily found as components of ADAPTOR PROTEIN COMPLEX 3 and ADAPTOR PROTEIN COMPLEX 4.
ADP-RIBOSYLATION FACTOR 1 is involved in regulating intracellular transport by modulating the interaction of coat proteins with organelle membranes in the early secretory pathway. It is a component of COAT PROTEIN COMPLEX I. This enzyme was formerly listed as EC 3.6.1.47.
Cell membranes associated with synapses. Both presynaptic and postsynaptic membranes are included along with their integral or tightly associated specializations for the release or reception of transmitters.
A fungal metabolite which is a macrocyclic lactone exhibiting a wide range of antibiotic activity.
Transport proteins that carry specific substances in the blood or across cell membranes.
MONOMERIC GTP-BINDING PROTEINS that were initially recognized as allosteric activators of the MONO(ADP-RIBOSE) TRANSFERASE of the CHOLERA TOXIN catalytic subunit. They are involved in vesicle trafficking and activation of PHOSPHOLIPASE D. This enzyme was formerly listed as EC 3.6.1.47
A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)
A replica technique in which cells are frozen to a very low temperature and cracked with a knife blade to expose the interior surfaces of the cells or cell membranes. The cracked cell surfaces are then freeze-dried to expose their constituents. The surfaces are now ready for shadowing to be viewed using an electron microscope. This method differs from freeze-fracturing in that no cryoprotectant is used and, thus, allows for the sublimation of water during the freeze-drying process to etch the surfaces.
The engulfing of liquids by cells by a process of invagination and closure of the cell membrane to form fluid-filled vacuoles.
An enzyme that catalyzes the hydrolysis of an alpha L-fucoside to yield an alcohol and L-fucose. Deficiency of this enzyme can cause FUCOSIDOSIS. EC 3.2.1.51.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Phosphoric acid esters of mannose.
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.
Changes in the amounts of various chemicals (neurotransmitters, receptors, enzymes, and other metabolites) specific to the area of the central nervous system contained within the head. These are monitored over time, during sensory stimulation, or under different disease states.
Multisubunit enzymes that reversibly synthesize ADENOSINE TRIPHOSPHATE. They are coupled to the transport of protons across a membrane.
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.
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.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
A family of proteins that play a role as cofactors in the process of CLATHRIN recycling in cells.
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.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
Membrane glycoproteins found in high concentrations on iron-utilizing cells. They specifically bind iron-bearing transferrin, are endocytosed with its ligand and then returned to the cell surface where transferrin without its iron is released.
Lipids, predominantly phospholipids, cholesterol and small amounts of glycolipids found in membranes including cellular and intracellular membranes. These lipids may be arranged in bilayers in the membranes with integral proteins between the layers and peripheral proteins attached to the outside. Membrane lipids are required for active transport, several enzymatic activities and membrane formation.
A group of enzymes which catalyze the hydrolysis of ATP. The hydrolysis reaction is usually coupled with another function such as transporting Ca(2+) across a membrane. These enzymes may be dependent on Ca(2+), Mg(2+), anions, H+, or DNA.
Enzymes that hydrolyze GTP to GDP. EC 3.6.1.-.
A family of small adaptin protein complex subunits of approximately 19 KDa in size.
Macromolecular complexes formed from the association of defined protein subunits.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
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)
A partitioning within cells due to the selectively permeable membranes which enclose each of the separate parts, e.g., mitochondria, lysosomes, etc.
Thin layers of tissue which cover parts of the body, separate adjacent cavities, or connect adjacent structures.
Hydrolases that specifically cleave the peptide bonds found in PROTEINS and PEPTIDES. Examples of sub-subclasses for this group include EXOPEPTIDASES and ENDOPEPTIDASES.
Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)
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.
An enzyme that catalyzes the HYDROLYSIS of terminal, non-reducing alpha-D-mannose residues in alpha-D-mannosides. The enzyme plays a role in the processing of newly formed N-glycans and in degradation of mature GLYCOPROTEINS. There are multiple isoforms of alpha-mannosidase, each having its own specific cellular location and pH optimum. Defects in the lysosomal form of the enzyme results in a buildup of mannoside intermediate metabolites and the disease ALPHA-MANNOSIDOSIS.
A narcotic analgesic morphinan used as a sedative in veterinary practice.
Separation of particles according to density by employing a gradient of varying densities. At equilibrium each particle settles in the gradient at a point equal to its density. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
A complex of polyene antibiotics obtained from Streptomyces filipinensis. Filipin III alters membrane function by interfering with membrane sterols, inhibits mitochondrial respiration, and is proposed as an antifungal agent. Filipins I, II, and IV are less important.
A clathrin adaptor protein complex primarily involved in clathrin-related transport at the TRANS-GOLGI NETWORK.
Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.
An enzyme isolated from horseradish which is able to act as an antigen. It is frequently used as a histochemical tracer for light and electron microscopy. Its antigenicity has permitted its use as a combined antigen and marker in experimental immunology.
Guanosine 5'-(tetrahydrogen triphosphate). A guanine nucleotide containing three phosphate groups esterified to the sugar moiety.
Established cell cultures that have the potential to propagate indefinitely.
A diverse class of enzymes that interact with UBIQUITIN-CONJUGATING ENZYMES and ubiquitination-specific protein substrates. Each member of this enzyme group has its own distinct specificity for a substrate and ubiquitin-conjugating enzyme. Ubiquitin-protein ligases exist as both monomeric proteins multiprotein complexes.
Glycoside hydrolases that catalyze the hydrolysis of alpha or beta linked MANNOSE.
An energy dependent process following the crosslinking of B CELL ANTIGEN RECEPTORS by multivalent ligands (bivalent anti-antibodies, LECTINS or ANTIGENS), on the B-cell surface. The crosslinked ligand-antigen receptor complexes collect in patches which flow to and aggregate at one pole of the cell to form a large mass - the cap. The caps may then be endocytosed or shed into the environment.
Branch-like terminations of NERVE FIBERS, sensory or motor NEURONS. Endings of sensory neurons are the beginnings of afferent pathway to the CENTRAL NERVOUS SYSTEM. Endings of motor neurons are the terminals of axons at the muscle cells. Nerve endings which release neurotransmitters are called PRESYNAPTIC TERMINALS.
Study of intracellular distribution of chemicals, reaction sites, enzymes, etc., by means of staining reactions, radioactive isotope uptake, selective metal distribution in electron microscopy, or other methods.
The adherence and merging of cell membranes, intracellular membranes, or artificial membranes to each other or to viruses, parasites, or interstitial particles through a variety of chemical and physical processes.
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.
A group of alicyclic hydrocarbons with the general formula R-C5H9.
A subtype of dynamin found primarily in the NEURONS of the brain.
Electrophoresis in which agar or agarose gel is used as the diffusion medium.
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to a choline moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and choline and 2 moles of fatty acids.
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.
Proteins that originate from plants species belonging to the genus ARABIDOPSIS. The most intensely studied species of Arabidopsis, Arabidopsis thaliana, is commonly used in laboratory experiments.
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.
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.
A representation, generally small in scale, to show the structure, construction, or appearance of something. (From Random House Unabridged Dictionary, 2d ed)
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
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.
Lipids containing one or more phosphate groups, particularly those derived from either glycerol (phosphoglycerides see GLYCEROPHOSPHOLIPIDS) or sphingosine (SPHINGOLIPIDS). They are polar lipids that are of great importance for the structure and function of cell membranes and are the most abundant of membrane lipids, although not stored in large amounts in the system.
A plant genus of the family BRASSICACEAE that contains ARABIDOPSIS PROTEINS and MADS DOMAIN PROTEINS. The species A. thaliana is used for experiments in classical plant genetics as well as molecular genetic studies in plant physiology, biochemistry, and development.
Layers of lipid molecules which are two molecules thick. Bilayer systems are frequently studied as models of biological membranes.
A C-type lectin that is a cell surface receptor for ASIALOGLYCOPROTEINS. It is found primarily in the LIVER where it mediates the endocytosis of serum glycoproteins.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
That portion of the electromagnetic spectrum in the visible, ultraviolet, and infrared range.
Techniques used to demonstrate or measure an immune response, and to identify or measure antigens using antibodies.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.
Centrifugation with a centrifuge that develops centrifugal fields of more than 100,000 times gravity. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
The threadlike, vascular projections of the chorion. Chorionic villi may be free or embedded within the DECIDUA forming the site for exchange of substances between fetal and maternal blood (PLACENTA).
Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
A hexosaminidase specific for non-reducing N-acetyl-D-hexosamine residues in N-acetyl-beta-D-hexosaminides. It acts on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES. Two specific mammalian isoenzymes of beta-N-acetylhexoaminidase are referred to as HEXOSAMINIDASE A and HEXOSAMINIDASE B. Deficiency of the type A isoenzyme causes TAY-SACHS DISEASE, while deficiency of both A and B isozymes causes SANDHOFF DISEASE. The enzyme has also been used as a tumor marker to distinguish between malignant and benign disease.
Iron-containing proteins that are widely distributed in animals, plants, and microorganisms. Their major function is to store IRON in a nontoxic bioavailable form. Each ferritin molecule consists of ferric iron in a hollow protein shell (APOFERRITINS) made of 24 subunits of various sequences depending on the species and tissue types.
Minute projections of cell membranes which greatly increase the surface area of the cell.
The movement of materials across cell membranes and epithelial layers against an electrochemical gradient, requiring the expenditure of metabolic energy.
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.
Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.
A superfamily of small proteins which are involved in the MEMBRANE FUSION events, intracellular protein trafficking and secretory processes. They share a homologous SNARE motif. The SNARE proteins are divided into subfamilies: QA-SNARES; QB-SNARES; QC-SNARES; and R-SNARES. The formation of a SNARE complex (composed of one each of the four different types SNARE domains (Qa, Qb, Qc, and R)) mediates MEMBRANE FUSION. Following membrane fusion SNARE complexes are dissociated by the NSFs (N-ETHYLMALEIMIDE-SENSITIVE FACTORS), in conjunction with SOLUBLE NSF ATTACHMENT PROTEIN, i.e., SNAPs (no relation to SNAP 25.)
The absence of light.
Any of various animals that constitute the family Suidae and comprise stout-bodied, short-legged omnivorous mammals with thick skin, usually covered with coarse bristles, a rather long mobile snout, and small tail. Included are the genera Babyrousa, Phacochoerus (wart hogs), and Sus, the latter containing the domestic pig (see SUS SCROFA).
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
An enzyme that catalyzes the hydrolysis of ACETYLCHOLINE to CHOLINE and acetate. In the CNS, this enzyme plays a role in the function of peripheral neuromuscular junctions. EC 3.1.1.7.
Techniques used to separate mixtures of substances based on differences in the relative affinities of the substances for mobile and stationary phases. A mobile phase (fluid or gas) passes through a column containing a stationary phase of porous solid or liquid coated on a solid support. Usage is both analytical for small amounts and preparative for bulk amounts.
A family of vesicular transport proteins characterized by an N-terminal transmembrane region and two C-terminal calcium-binding domains.
A class of MOLECULAR CHAPERONES found in both prokaryotes and in several compartments of eukaryotic cells. These proteins can interact with polypeptides during a variety of assembly processes in such a way as to prevent the formation of nonfunctional structures.
The distal terminations of axons which are specialized for the release of neurotransmitters. Also included are varicosities along the course of axons which have similar specializations and also release transmitters. Presynaptic terminals in both the central and peripheral nervous systems are included.
The process of cleaving a chemical compound by the addition of a molecule of water.
Enzymes that catalyze the hydrolysis of N-acylhexosamine residues in N-acylhexosamides. Hexosaminidases also act on GLUCOSIDES; GALACTOSIDES; and several OLIGOSACCHARIDES.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
The region of the stem beneath the stalks of the seed leaves (cotyledons) and directly above the young root of the embryo plant. It grows rapidly in seedlings showing epigeal germination and lifts the cotyledons above the soil surface. In this region (the transition zone) the arrangement of vascular bundles in the root changes to that of the stem. (From Concise Dictionary of Biology, 1990)
A POSTURE in which an ideal body mass distribution is achieved. Postural balance provides the body carriage stability and conditions for normal functions in stationary position or in movement, such as sitting, standing, or walking.
A family of structurally related proteins that were originally discovered for their role in cell-cycle regulation in CAENORHABDITIS ELEGANS. They play important roles in regulation of the CELL CYCLE and as components of UBIQUITIN-PROTEIN LIGASES.
A chromatographic technique that utilizes the ability of biological molecules to bind to certain ligands specifically and reversibly. It is used in protein biochemistry. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Artificially produced membranes, such as semipermeable membranes used in artificial kidney dialysis (RENAL DIALYSIS), monomolecular and bimolecular membranes used as models to simulate biological CELL MEMBRANES. These membranes are also used in the process of GUIDED TISSUE REGENERATION.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
The outer layer of the adrenal gland. It is derived from MESODERM and comprised of three zones (outer ZONA GLOMERULOSA, middle ZONA FASCICULATA, and inner ZONA RETICULARIS) with each producing various steroids preferentially, such as ALDOSTERONE; HYDROCORTISONE; DEHYDROEPIANDROSTERONE; and ANDROSTENEDIONE. Adrenal cortex function is regulated by pituitary ADRENOCORTICOTROPIN.
Conjugated protein-carbohydrate compounds including mucins, mucoid, and amyloid glycoproteins.
A large family of MONOMERIC GTP-BINDING PROTEINS that play a key role in cellular secretory and endocytic pathways. EC 3.6.1.-.
A family of synaptic vesicle-associated proteins involved in the short-term regulation of NEUROTRANSMITTER release. Synapsin I, the predominant member of this family, links SYNAPTIC VESICLES to ACTIN FILAMENTS in the presynaptic nerve terminal. These interactions are modulated by the reversible PHOSPHORYLATION of synapsin I through various signal transduction pathways. The protein is also a substrate for cAMP- and CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASES. It is believed that these functional properties are also shared by synapsin II.
Neurotoxic proteins from the venom of the banded or Formosan krait (Bungarus multicinctus, an elapid snake). alpha-Bungarotoxin blocks nicotinic acetylcholine receptors and has been used to isolate and study them; beta- and gamma-bungarotoxins act presynaptically causing acetylcholine release and depletion. Both alpha and beta forms have been characterized, the alpha being similar to the large, long or Type II neurotoxins from other elapid venoms.
Immunoglobulin molecules having a specific amino acid sequence by virtue of which they interact only with the ANTIGEN (or a very similar shape) that induced their synthesis in cells of the lymphoid series (especially PLASMA CELLS).
A subfamily of Q-SNARE PROTEINS which occupy the same position as syntaxin 1A in the SNARE complex and which also are most similar to syntaxin 1A in their AMINO ACID SEQUENCE. This subfamily is also known as the syntaxins, although a few so called syntaxins are Qc-SNARES.
A highly vascularized mammalian fetal-maternal organ and major site of transport of oxygen, nutrients, and fetal waste products. It includes a fetal portion (CHORIONIC VILLI) derived from TROPHOBLASTS and a maternal portion (DECIDUA) derived from the uterine ENDOMETRIUM. The placenta produces an array of steroid, protein and peptide hormones (PLACENTAL HORMONES).
The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.
Proteins found in plants (flowers, herbs, shrubs, trees, etc.). The concept does not include proteins found in vegetables for which VEGETABLE PROTEINS is available.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
A serine endopeptidase that is formed from TRYPSINOGEN in the pancreas. It is converted into its active form by ENTEROPEPTIDASE in the small intestine. It catalyzes hydrolysis of the carboxyl group of either arginine or lysine. EC 3.4.21.4.
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.
Two-phase systems in which one is uniformly dispersed in another as particles small enough so they cannot be filtered or will not settle out. The dispersing or continuous phase or medium envelops the particles of the discontinuous phase. All three states of matter can form colloids among each other.
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.
Cell surface proteins that bind acetylcholine with high affinity and trigger intracellular changes influencing the behavior of cells. Cholinergic receptors are divided into two major classes, muscarinic and nicotinic, based originally on their affinity for nicotine and muscarine. Each group is further subdivided based on pharmacology, location, mode of action, and/or molecular biology.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
The developmental entity of a fertilized chicken egg (ZYGOTE). The developmental process begins about 24 h before the egg is laid at the BLASTODISC, a small whitish spot on the surface of the EGG YOLK. After 21 days of incubation, the embryo is fully developed before hatching.
Contractile tissue that produces movement in animals.
A cyclododecadepsipeptide ionophore antibiotic produced by Streptomyces fulvissimus and related to the enniatins. It is composed of 3 moles each of L-valine, D-alpha-hydroxyisovaleric acid, D-valine, and L-lactic acid linked alternately to form a 36-membered ring. (From Merck Index, 11th ed) Valinomycin is a potassium selective ionophore and is commonly used as a tool in biochemical studies.
Electron microscopy in which the ELECTRONS or their reaction products that pass down through the specimen are imaged below the plane of the specimen.
A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels.
Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.
An interstitial lung disease of unknown etiology, occurring between 21-80 years of age. It is characterized by a dramatic onset of a "pneumonia-like" illness with cough, fever, malaise, fatigue, and weight loss. Pathological features include prominent interstitial inflammation without collagen fibrosis, diffuse fibroblastic foci, and no microscopic honeycomb change. There is excessive proliferation of granulation tissue within small airways and alveolar ducts.
Agents that emit light after excitation by light. The wave length of the emitted light is usually longer than that of the incident light. Fluorochromes are substances that cause fluorescence in other substances, i.e., dyes used to mark or label other compounds with fluorescent tags.
A type of extracellular vesicle, containing RNA and proteins, that is secreted into the extracellular space by EXOCYTOSIS when MULTIVESICULAR BODIES fuse with the PLASMA MEMBRANE.
Derivatives of ammonium compounds, NH4+ Y-, in which all four of the hydrogens bonded to nitrogen have been replaced with hydrocarbyl groups. These are distinguished from IMINES which are RN=CR2.
Cells that store epinephrine secretory vesicles. During times of stress, the nervous system signals the vesicles to secrete their hormonal content. Their name derives from their ability to stain a brownish color with chromic salts. Characteristically, they are located in the adrenal medulla and paraganglia (PARAGANGLIA, CHROMAFFIN) of the sympathetic nervous system.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Substances used for their pharmacological actions on any aspect of neurotransmitter systems. Neurotransmitter agents include agonists, antagonists, degradation inhibitors, uptake inhibitors, depleters, precursors, and modulators of receptor function.
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.
A vesicular transport protein expressed predominately in NEURONS. Synaptotagmin helps regulate EXOCYTOSIS of SYNAPTIC VESICLES and appears to serve as a calcium sensor to trigger NEUROTRANSMITTER release. It also acts as a nerve cell receptor for certain BOTULINUM TOXINS.
The communication from a NEURON to a target (neuron, muscle, or secretory cell) across a SYNAPSE. In chemical synaptic transmission, the presynaptic neuron releases a NEUROTRANSMITTER that diffuses across the synaptic cleft and binds to specific synaptic receptors, activating them. The activated receptors modulate specific ion channels and/or second-messenger systems in the postsynaptic cell. In electrical synaptic transmission, electrical signals are communicated as an ionic current flow across ELECTRICAL SYNAPSES.
The property of objects that determines the direction of heat flow when they are placed in direct thermal contact. The temperature is the energy of microscopic motions (vibrational and translational) of the particles of atoms.
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.
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to a serine moiety. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid and serine and 2 moles of fatty acids.
The primary plant photoreceptor responsible for perceiving and mediating responses to far-red light. It is a PROTEIN-SERINE-THREONINE KINASE that is translocated to the CELL NUCLEUS in response to light signals.
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.
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.
Specialized junctions at which a neuron communicates with a target cell. At classical synapses, a neuron's presynaptic terminal releases a chemical transmitter stored in synaptic vesicles which diffuses across a narrow synaptic cleft and activates receptors on the postsynaptic membrane of the target cell. The target may be a dendrite, cell body, or axon of another neuron, or a specialized region of a muscle or secretory cell. Neurons may also communicate via direct electrical coupling with ELECTRICAL SYNAPSES. Several other non-synaptic chemical or electric signal transmitting processes occur via extracellular mediated interactions.
A microtubule subunit protein found in large quantities in mammalian brain. It has also been isolated from SPERM FLAGELLUM; CILIA; and other sources. Structurally, the protein is a dimer with a molecular weight of approximately 120,000 and a sedimentation coefficient of 5.8S. It binds to COLCHICINE; VINCRISTINE; and VINBLASTINE.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
A large superfamily of transcription factors that contain a region rich in BASIC AMINO ACID residues followed by a LEUCINE ZIPPER domain.
The pressure required to prevent the passage of solvent through a semipermeable membrane that separates a pure solvent from a solution of the solvent and solute or that separates different concentrations of a solution. It is proportional to the osmolality of the solution.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in plants.
A nitrogen-free class of lipids present in animal and particularly plant tissues and composed of one mole of glycerol and 1 or 2 moles of phosphatidic acid. Members of this group differ from one another in the nature of the fatty acids released on hydrolysis.
A blue-green biliprotein widely distributed in the plant kingdom.

Clathrin and two components of the COPII complex, Sec23p and Sec24p, could be involved in endocytosis of the Saccharomyces cerevisiae maltose transporter. (1/342)

The Saccharomyces cerevisiae maltose transporter is a 12-transmembrane segment protein that under certain physiological conditions is degraded in the vacuole after internalization by endocytosis. Previous studies showed that endocytosis of this protein is dependent on the actin network, is independent of microtubules, and requires the binding of ubiquitin. In this work, we attempted to determine which coat proteins are involved in this endocytosis. Using mutants defective in the heavy chain of clathrin and in several subunits of the COPI and the COPII complexes, we found that clathrin, as well as two cytosolic subunits of COPII, Sec23p and Sec24p, could be involved in internalization of the yeast maltose transporter. The results also indicate that endocytosis of the maltose transporter and of the alpha-factor receptor could have different requirements.  (+info)

LST1 is a SEC24 homologue used for selective export of the plasma membrane ATPase from the endoplasmic reticulum. (2/342)

In Saccharomyces cerevisiae, vesicles that carry proteins from the ER to the Golgi compartment are encapsulated by COPII coat proteins. We identified mutations in ten genes, designated LST (lethal with sec-thirteen), that were lethal in combination with the COPII mutation sec13-1. LST1 showed synthetic-lethal interactions with the complete set of COPII genes, indicating that LST1 encodes a new COPII function. LST1 codes for a protein similar in sequence to the COPII subunit Sec24p. Like Sec24p, Lst1p is a peripheral ER membrane protein that binds to the COPII subunit Sec23p. Chromosomal deletion of LST1 is not lethal, but inhibits transport of the plasma membrane proton-ATPase (Pma1p) to the cell surface, causing poor growth on media of low pH. Localization by both immunofluorescence microscopy and cell fractionation shows that the export of Pma1p from the ER is impaired in lst1Delta mutants. Transport of other proteins from the ER was not affected by lst1Delta, nor was Pma1p transport found to be particularly sensitive to other COPII defects. Together, these findings suggest that a specialized form of the COPII coat subunit, with Lst1p in place of Sec24p, is used for the efficient packaging of Pma1p into vesicles derived from the ER.  (+info)

Identification of the putative mammalian orthologue of Sec31P, a component of the COPII coat. (3/342)

The regulation of intracellular vesicular trafficking is mediated by specific families of proteins that are involved in vesicular budding, translocation, and fusion with target membranes. We purified a vesicle-associated protein from hepatic microsomes using sequential column chromatography and partially sequenced it. Oliogonucleotides based on these sequences were used to clone the protein from a rat liver cDNA library. The clone encoded a novel protein with a predicted mass of 137 kDa (p137). The protein had an N terminus WD repeat motif with significant homology to Sec31p, a member of the yeast COPII coat that complexes with Sec13p. We found that p137 interacted with mammalian Sec13p using several approaches: co-elution through sequential column chromatography, co-immunoprecipitation from intact cells, and yeast two-hybrid analysis. Morphologically, the p137 protein was localized to small punctate structures in the cytoplasm of multiple cultured cell lines. When Sec13p was transfected into these cells, it demonstrated considerable overlap with p137. This overlap was maintained through several pharmacological manipulations. The p137 compartment also demonstrated partial overlap with ts045-VSVG protein when infected cells were incubated at 15 degrees C. These findings suggest that p137 is the mammalian orthologue of Sec31p.  (+info)

Sec24p and Iss1p function interchangeably in transport vesicle formation from the endoplasmic reticulum in Saccharomyces cerevisiae. (4/342)

The Sec23p/Sec24p complex functions as a component of the COPII coat in vesicle transport from the endoplasmic reticulum. Here we characterize Saccharomyces cerevisiae SEC24, which encodes a protein of 926 amino acids (YIL109C), and a close homologue, ISS1 (YNL049C), which is 55% identical to SEC24. SEC24 is essential for vesicular transport in vivo because depletion of Sec24p is lethal, causing exaggeration of the endoplasmic reticulum and a block in the maturation of carboxypeptidase Y. Overproduction of Sec24p suppressed the temperature sensitivity of sec23-2, and overproduction of both Sec24p and Sec23p suppressed the temperature sensitivity of sec16-2. SEC24 gene disruption could be complemented by overexpression of ISS1, indicating functional redundancy between the two homologous proteins. Deletion of ISS1 had no significant effect on growth or secretion; however, iss1Delta mutants were found to be synthetically lethal with mutations in the v-SNARE genes SEC22 and BET1. Moreover, overexpression of ISS1 could suppress mutations in SEC22. These genetic interactions suggest that Iss1p may be specialized for the packaging or the function of COPII v-SNAREs. Iss1p tagged with His(6) at its C terminus copurified with Sec23p. Pure Sec23p/Iss1p could replace Sec23p/Sec24p in the packaging of a soluble cargo molecule (alpha-factor) and v-SNAREs (Sec22p and Bet1p) into COPII vesicles. Abundant proteins in the purified vesicles produced with Sec23p/Iss1p were indistinguishable from those in the regular COPII vesicles produced with Sec23p/Sec24p.  (+info)

Sfb2p, a yeast protein related to Sec24p, can function as a constituent of COPII coats required for vesicle budding from the endoplasmic reticulum. (5/342)

The COPII coat is required for vesicle budding from the endoplasmic reticulum (ER), and consists of two heterodimeric subcomplexes, Sec23p/Sec24p, Sec13p/Sec31p, and a small GTPase, Sar1p. We characterized a yeast mutant, anu1 (abnormal nuclear morphology) exhibiting proliferated ER as well as abnormal nuclear morphology at the restrictive temperature. Based on the finding that ANU1 is identical to SEC24, we confirmed a temperature-sensitive protein transport from the ER to the Golgi in anu1-1/sec24-20 cells. Overexpression of SFB2, a SEC24 homologue with 56% identity, partially suppressed not only the mutant phenotype of sec24-20 cells but also rescued the SEC24-disrupted cells. Moreover, the yeast two-hybrid assay revealed that Sfb2p, similarly to Sec24p, interacted with Sec23p. In SEC24-disrupted cells rescued by overexpression of SFB2, some cargo proteins were still retained in the ER, while most of the protein transport was restored. Together, these findings strongly suggest that Sfb2p functions as the component of COPII coats in place of Sec24p, and raise the possibility that each member of the SEC24 family of proteins participates directly and/or indirectly in cargo-recognition events with its own cargo specificity at forming ER-derived vesicles.  (+info)

Mutants affecting the structure of the cortical endoplasmic reticulum in Saccharomyces cerevisiae. (6/342)

We find that the peripheral ER in Saccharomyces cerevisiae forms a dynamic network of interconnecting membrane tubules throughout the cell cycle, similar to the ER in higher eukaryotes. Maintenance of this network does not require microtubule or actin filaments, but its dynamic behavior is largely dependent on the actin cytoskeleton. We isolated three conditional mutants that disrupt peripheral ER structure. One has a mutation in a component of the COPI coat complex, which is required for vesicle budding. This mutant has a partial defect in ER segregation into daughter cells and disorganized ER in mother cells. A similar phenotype was found in other mutants with defects in vesicular trafficking between ER and Golgi complex, but not in mutants blocked at later steps in the secretory pathway. The other two mutants found in the screen have defects in the signal recognition particle (SRP) receptor. This receptor, along with SRP, targets ribosome-nascent chain complexes to the ER membrane for protein translocation. A conditional mutation in SRP also disrupts ER structure, but other mutants with translocation defects do not. We also demonstrate that, both in wild-type and mutant cells, the ER and mitochondria partially coalign, and that mutations that disrupt ER structure also affect mitochondrial structure. Our data suggest that both trafficking between the ER and Golgi complex and ribosome targeting are important for maintaining ER structure, and that proper ER structure may be required to maintain mitochondrial structure.  (+info)

Kinase signaling initiates coat complex II (COPII) recruitment and export from the mammalian endoplasmic reticulum. (7/342)

The events regulating coat complex II (COPII) vesicle formation involved in the export of cargo from the endoplasmic reticulum (ER) are unknown. COPII recruitment to membranes is initiated by the activation of the small GTPase Sar1. We have utilized purified COPII components in both membrane recruitment and cargo export assays to analyze the possible role of kinase regulation in ER export. We now demonstrate that Sar1 recruitment to membranes requires ATP. We find that the serine/threonine kinase inhibitor H89 abolishes membrane recruitment of Sar1, thereby preventing COPII polymerization by interfering with the recruitment of the cytosolic Sec23/24 COPII coat complex. Inhibition of COPII recruitment prevents export of cargo from the ER. These results demonstrate that ER export and initiation of COPII vesicle formation in mammalian cells is under kinase regulation.  (+info)

The p58-positive pre-golgi intermediates consist of distinct subpopulations of particles that show differential binding of COPI and COPII coats and contain vacuolar H(+)-ATPase. (8/342)

We have studied the structural and functional properties of the pre-Golgi intermediate compartment (IC) in normal rat kidney cells using analytical cell fractionation with p58 as the principal marker. The sedimentation profile (sediterm) of p58, obtained by analytical differential centrifugation, revealed in steady-state cells the presence of two main populations of IC elements whose average sedimentation coefficients, s(H)=1150+/-58S ('heavy') and s(L)=158+/-8S ('light'), differed from the s-values obtained for elements of the rough and smooth endoplasmic reticulum. High resolution analysis of these subpopulations in equilibrium density gradients further revealed that the large difference in their s-values was mainly due to particle size. The 'light' particle population contained the bulk of COPI and COPII coats, and redistribution of p58 to these particles was observed in transport-arrested cells, showing that the two types of elements are also compositionally distinct and have functional counterparts in intact cells. Using a specific antibody against the 16 kDa proteolipid subunit of the vacuolar H(+)-ATPase, an enrichment of the V(o )domain of the ATPase was observed in the p58-positive IC elements. Interestingly, these elements could contain both COPI and COPII coats and their density distribution was markedly affected by GTP(&ggr;)S. Together with morphological observations, these results demonstrate that, in addition to clusters of small tubules and vesicles, the IC also consists of large-sized structures and corroborate the proposal that the IC elements contain an active vacuolar H(+)-ATPase.  (+info)

Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum. This protein is required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers. It may participate in cargo loading of COL7A1 at endoplasmic reticulum exit sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing carrier. Does not play a role in global protein secretion and is apparently specific to COL7A1 cargo loading. However, it may participate in secretion of other proteins in cells that do not secrete COL7A1. It is also specifically required for the secretion of lipoproteins by participating in their export from the endoplasmic reticulum (PubMed:27138255 ...
Transport and Golgi organization protein 1 homolog; Plays a role in the transport of cargos that are too large to fit into COPII-coated vesicles and require specific mechanisms to be incorporated into membrane-bound carriers and exported from the endoplasmic reticulum. This protein is required for collagen VII (COL7A1) secretion by loading COL7A1 into transport carriers. It may participate in cargo loading of COL7A1 at endoplasmic reticulum exit sites by binding to COPII coat subunits Sec23/24 and guiding SH3-bound COL7A1 into a growing carrier. Does not play a role in global protein s ...
In this study, we showed that Sec12 recruitment to ER exit sites by interactions with cTAGE5 is necessary for collagen transport from the ER. As the interaction between cTAGE5 and Sec12 did not alter the activity of Sec12 toward Sar1, cTAGE5-mediated Sec12 concentration may be important for the localized activation of Sar1 in the vicinity of the ER exit sites. In this regard, it has been reported that Sedlin is somehow involved in the inactivation of Sar1 through interaction with TANGO1 at ER exit sites and is specifically required for collagen secretion (Venditti et al., 2012). Thus, it is interesting to speculate that the exit of collagen from the ER may rely on specific activation-inactivation mechanisms-Sar1 might first be activated by the cTAGE5-Sec12 complex and then inactivated by TANGO1-Sedlin. In this case, tight regulation of the Sar1 GTPase cycle at ER exit sites would be important for collagen secretion from the ER, although we cannot totally rule out the possibility that ...
TY - JOUR. T1 - PCTAIRE protein kinases interact directly with the COPII complex and modulate secretory cargo transport. AU - Palmer, KJ. AU - Konkel, JE. AU - Stephens, DJ. N1 - Publisher: Company of Biologists Other: Konkel, JE was a third year Bristol Biochemistry student and Nuffield summer student. PY - 2005/9. Y1 - 2005/9. U2 - 10.1242/jcs.02496. DO - 10.1242/jcs.02496. M3 - Article (Academic Journal). VL - 118 (17). SP - 3839. EP - 3847. JO - Journal of Cell Science. JF - Journal of Cell Science. SN - 0021-9533. ER - ...
Protein trafficking from the endoplasmic reticulum (ER) to the Golgi apparatus involves specific uptake into coat protein complex II (COPII)-coated vesicles of secretory and of vesicle targeting (v-SNARE) proteins. Here, two ER to Golgi v-SNAREs, Bet1p and Bos1p, were shown to interact specifically with Sar1p, Sec23p, and Sec24p, components of the COPII coat, in a guanine nucleotide-dependent fashion. Other v-SNAREs, Sec22p and Ykt6p, might interact more weakly with the COPII coat or interact indirectly by binding to Bet1p or Bos1p. The data suggest that transmembrane proteins can be taken up into COPII vesicles by direct interactions with the coat proteins and may play a structural role in the assembly of the COPII coat complex. ...
Plant Golgi stacks are mobile organelles that can travel along actin filaments. How COPII (coat complex II) vesicles are transferred from endoplasmic reticulum (ER) export sites to the moving Golgi stacks is not understood. We have examined COPII vesicle transfer in high-pressure frozen/freeze-subst …
Marian Blanca Ramírez from the CSIC in Spain has been studying the effects of LRRK2, a protein associated with Parkinsons disease, on cell motility. A Travelling Fellowship from Journal of Cell Science allowed her to spend time in Prof Maddy Parsons lab at Kings College London, learning new cell migration assays and analysing fibroblasts cultured from individuals with Parkinsons. Read more on her story here. Where could your research take you? The deadline to apply for the current round of Travelling Fellowships is 23rd Feburary 2018. Apply now!. ...
Collagen is the most abundant protein in the animal kingdom. It is of fundamental importance during development for cell differentiation and tissue morphogenesis as well as in pathological processes such as fibrosis and cancer cell migration. However, our understanding of the mechanisms of procollagen secretion remains limited. Here, we show that TFG organizes transitional ER (tER) and ER exit sites (ERESs) into larger structures. Depletion of TFG results in dispersion of tER elements that remain associated with individual ER-Golgi intermediate compartments (ERGICs) as largely functional ERESs. We show that TFG is not required for the transport and packaging of small soluble cargoes but is necessary for the export of procollagen from the ER. Our work therefore suggests a key relationship between the structure and function of ERESs and a central role for TFG in optimizing COPII assembly for procollagen export ...
Component of the coat protein complex II (COPII) which promotes the formation of transport vesicles from the endoplasmic reticulum (ER). The coat has two main functions, the physical deformation of the endoplasmic reticulum membrane into vesicles and the selection of cargo molecules.
On page 1029, Supek et al. illustrate how a peripheral membrane protein organizes a coat protein complex involved in secretory vesicle formation.. The protein in question, yeast Sec16p, is an ER resident required in vivo for COPII-dependent vesicle budding. In vitro, Sec16p is not necessary for budding from liposomes reconstituted with pure cytosolic COPII proteins. However, this in vitro reaction depends on a nonhydrolyzable form of GTP, probably because the COPII coat falls apart when Sar1p (the initiator of coat assembly) hydrolyzes GTP. Until now, the function of Sec16p in liposome budding could not be tested, because the protein was difficult to purify. Supek et al. report conditions that stabilize Sec16p and have purified enough protein for in vitro studies. Microsomal membranes stripped of endogenous Sec16p were stimulated in vesicle budding by the purified. protein, but only in the presence of hydrolyzable GTP. Thus, the in vivo function of Sec16p may be either to slow GTP hydrolysis ...
Collagen is the most abundant protein in the animal kingdom. It is of fundamental importance during development for cell differentiation and tissue morphogenesis as well as in pathological processes such as fibrosis and cancer cell migration. However, our understanding of the mechanisms of procollag …
CiteSeerX - Document Details (Isaac Councill, Lee Giles, Pradeep Teregowda): Abstract. COPII-coated ER-derived transport vesicles from Saccharomyces cerevisiae contain a distinct set of membrane-bound polypeptides. One of these polypeptides, termed Erv14p (ER-vesicle protein of 14 kD), corresponds to an open reading frame on yeast chromosome VII that is predicted to encode an integral membrane protein and shares sequence identity with the Drosophila cornichon gene product. Experiments with an epitope-tagged version of Erv14p indicate that this protein localizes to the ER and is selectively packaged into COPII-coated vesicles. Haploid cells that lack Erv14p are viable but display a modest defect in bud site selection because a transmembrane secretory protein, Axl2p, is not efficiently delivered to the cell surface. Axl2p is required for selection of axial growth
Pandey A, Fernandez MM, Steen H, Blagoev B, Nielsen MM, Roche S, Mann M, Lodish HF. Identification of a novel immunoreceptor tyrosine-based activation motif-containing molecule, STAM2, by mass spectrometry and its involvement in growth factor and cytokine receptor signaling pathways. J Biol Chem 2000;275:38633-38639 ...
Structural Component Of 3 Distinct Complexes; Subunit Of Nup84 Nuclear Pore Sub-complex (NPC), COPII Vesicle Coat, And Seh1-associated (SEA) Complex; COPII Vesicle Coat Is Required For ER To Golgi Transport; The Nup84 Subcomplex Contributes To Nucleocytoplasmic Transport, NPC Biogenesis And Processes That May Require Localization Of Chromosomes At The Nuclear Periphery, Including Transcription; Homologous To Human SEC13; Abundance Increases Under DNA Replication Stress
Structural component of 3 distinct complexes; subunit of Nup84 nuclear pore sub-complex (NPC), COPII vesicle coat, and Seh1-associated (SEA) complex; COPII vesicle coat is required for ER to Golgi transport; the Nup84 subcomplex contributes to nucleocytoplasmic transport, NPC biogenesis and processes that may require localization of chromosomes at the nuclear periphery, including transcription; homologous to human SEC13; abundance increases under DNA replication stress ...
Structural component of 3 distinct complexes; subunit of Nup84 nuclear pore sub-complex (NPC), COPII vesicle coat, and Seh1-associated (SEA) complex; COPII vesicle coat is required for ER to Golgi transport; the Nup84 subcomplex contributes to nucleocytoplasmic transport, NPC biogenesis and processes that may require localization of chromosomes at the nuclear periphery, including transcription; homologous to human SEC13; abundance increases under DNA replication stress ...
This API will return progress of a previous POST request to /v4/tir/gdpr/export/{site_uuid}/{thirdparty_id}/{thirdparty_provider} The response will be in the form of progress status or a final result containing the exported data. ...
The budding process if as follows (Figure 9). Sar1p goes to the ER. Sec12p converts Sar1p-GDP to the activated GTP-bound form. This causes Sar1p to be membrane-bound. GTP is the best nucleotide for budding. Then, Sar1p-GTP recruits Sec23p and Sec13p complexes to form COPII. COPII executes the budding event. Sar1p hydrolyzes GTP, stimulated by the Sec23p subunit of the Sec23p complex. GTP hydrolysis leads to the loss of Sar1p from vesicles, causing coat instability. The Sar1p loss exposes targeting proteins on the vesicle, such as Sec22p and Bos1p. These proteins provide binding selectivity to the target proteins on the Golgi membrane. If vesicles form with a nonhydrolyzable analog like GMP-PNP, Sar1p and the COPII proteins remain on the vesicle (Figure 8). The remaining Sar1p and COPII proteins hinder access of the vesicle to the Golgi. The vesicle will not be able to fuse with the acceptor membrane.. COPII formation resembles the assembly of COPI. But, COPI and COPII are distinct. Unlike COPI, ...
These reference sequences exist independently of genome builds. Explain. These reference sequences are curated independently of the genome annotation cycle, so their versions may not match the RefSeq versions in the current genome build. Identify version mismatches by comparing the version of the RefSeq in this section to the one reported in Genomic regions, transcripts, and products above. ...
Member Of The P24 Family Involved In ER To Golgi Transport; Similar To Emp24p And Erv25p; Role In Misfolded Protein Quality Control; Forms A Heterotrimeric Complex With Erp1p, Emp24p, And Erv25p; Localized To COPII-coated Vesicles; ERP2 Has A Paralog, ERP4, That Arose From The Whole Genome Duplication
Synonyms for E (exit) site in Free Thesaurus. Antonyms for E (exit) site. 3 words related to ribosome: cell organ, cell organelle, organelle. What are synonyms for E (exit) site?
Precise inheritance of organelles during mitosis ensures the proper organisation and function of daughter cells. Inheritance of the Golgi complex, a single copy organelle, requires its disassembly before mitosis; Golgi disassembly is driven by mitotic inhibition of COPII-dependent export of proteins from endoplasmic reticulum exit sites (ERESs) to the Golgi. Helen Hughes and David Stephens have been investigating how ERESs are restored at the end of mitosis and, on page 4032, they report that Sec16A - the major human orthologue of Sec16, which defines the site of COPII vesicle budding in yeast - defines the site at which COPII-dependent budding reinitiates after mitosis. Using quantitative 4D imaging of HeLa cells stably expressing fluorescently labelled Sec16A, the authors show that, unlike all other COPII components, Sec16A remains associated with ERESs throughout mitosis. Moreover, Sec16A localisation is coincident with the reappearance of COPII puncta on mitotic exit. Hughes and Stephens ...
p,Coat protein I (COPI)-coated vesicles mediate retrograde transport from the Golgi to the endoplasmic reticulum (ER), as well as transport within the Golgi. Major progress has been made in defining the structure of COPI coats, in vitro and in vivo, at resolutions as high as 9 Å. Nevertheless, important questions remain unanswered, including what specific interactions stabilize COPI coats, how COPI vesicles recognize their target membranes, and how coat disassembly is coordinated with vesicle fusion and cargo delivery. Here, we use X-ray crystallography to identify a conserved site on the COPI subunit α-COP that binds to flexible, acidic sequences containing a single tryptophan residue. One such sequence, found within α-COP itself, mediates α-COP homo-oligomerization. Another such sequence is contained within the lasso of the ER-resident Dsl1 complex, where it helps mediate the tethering of Golgi-derived COPI vesicles at the ER membrane. Together, our findings suggest that α-COP ...
Exit sites (ES) are specialized domains of the endoplasmic reticulum (ER) at which cargo proteins of the secretory pathway are packaged into COPII-coated vesicles. Although the essential COPII proteins (Sar1p, Sec23p-Sec24p, Sec13p-Sec31p) have been characterized in detail and their sequential binding kinetics at ER membranes have been quantified, the basic processes that govern the self-assembly and spatial organization of ERES have remained elusive. Here, we have formulated a generic computational model that describes the process of formation of ERES on a mesoscopic scale. The model predicts that ERES are arranged in a quasi-crystalline pattern, while their size strongly depends on the cargo-modulated kinetics of COPII turnover - that is, a lack of cargo leads to smaller and more mobile ERES. These predictions are in favorable agreement with experimental data obtained by fluorescence microscopy. The model further suggests that cooperative binding of COPII components, for example mediated by regulatory
Peng, R.; Grabowski, R.; De Antoni, A.; Gallwitz, D.: Specific interaction of the yeast cis-Golgi syntaxin Sed5p and the coat protein complex II component Sec24p of endoplasmic reticulum-derived transport vesicles. Proceedings of the National Academy of Sciences USA 96, pp. 3751 - 3756 (1999 ...
The nucleus is one of the defining features of eukaryotes and the question of its origin is intimately linked to the evolution of the eukaryotic cell. It is delimited by a double lipid bilayer called the nuclear envelope, which separates the nuclear interior from the cytoplasm. The inner and outer membranes of the nucleus are continuous with one another creating a single folded envelope, interrupted by nuclear pore complexes (NPCs), which enable transport of proteins and RNA between nucleoplasm and cytoplasm.. A combination of proteomic and bioinformatic analyses has shown that numerous Nups are conserved between yeast and vertebrates. As this only describes a subset of eukaryotic diversity, comparative genomic analyses were used to establish the extent to which the NPC is conserved across the eukaryotic tree. NPCs have been suggested to share a common origin with vesicle coat proteins of the endomembrane system. An additional goal of this work was therefore to establish the distribution of ...
Coatomer coated (COPI) vesicles play a pivotal role for multiple membrane trafficking steps throughout the eukaryotic cell. Our focus is on betaCOP, one of the most well known components of the COPI multi-protein complex. Amino acid differences in be
Author: Rein, U. et al.; Genre: Journal Article; Published in Print: 2002-04-29; Open Access; Keywords: Arf; ARF-GAP; COPI; ER-Golgi SNAREs; protein transport|br/|; Title: ARF-GAP-mediated interaction between the ER-Golgi v-SNAREs and the COPI coat
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The protein encoded by this gene is reported to be a component of the Golgi matrix. It may act as a golgin protein by negatively regulating transit of secretory cargo and by acting as a structural scaffold of the Golgi. Alternative splicing results in multiple transcript variants ...
The protein encoded by this gene is reported to be a component of the Golgi matrix. It may act as a golgin protein by negatively regulating transit of secretory cargo and by acting as a structural scaffold of the Golgi. Alternative splicing results in multiple transcript variants ...
TY - JOUR. T1 - Tethering assays for COPI vesicles mediated by golgins. AU - Satoh, Ayano. AU - Malsam, Jörg. AU - Warren, Graham. N1 - Funding Information: We thank all members of the Warren, Mellman, and Toomre laboratories for helpful comments and discussions, and Marino Zerial for generous provision of purified EEA1. This work was supported by the NIH and the Ludwig Institute for Cancer Research. A.S. was supported by the American Heart Association.. PY - 2005. Y1 - 2005. N2 - A method is described that allows the attachment of COPI vesicles and Golgi membranes to glass slides that can then be analyzed using electron microscopy (EM) and immuno-EM methods. Subpopulations of COPI vesicles can be bound selectively using recombinant golgins. Alternatively, COPI vesicles can be attached to prebound Golgi membranes. Marking these vesicles selectively with biotin allows their site of attachment to be identified.. AB - A method is described that allows the attachment of COPI vesicles and Golgi ...
Transport vesicles form at a donor compartment and fuse to an acceptor compartment mediate the movement of cargo proteins within eukaryotic cells from one subcellular compartment to another. COPII vesicles specifically provide the means of transport for proteins from the endoplasmic reticulum (ER) to the Golgi apparatus. The in vitro enrichment of COPII vesicles was undertaken with the intent of better understanding COPII dependent transport between the ER and Golgi. This approach allowed for the identification of abundant vesicle proteins, one of which is Erv14p, an ER-vesicle protein of 14 kDa. Erv14p is an integral membrane protein that localized to the ER and Golgi and was responsible for the efficient transport of at least one secretory cargo protein, Ax12p. Erv14p was not essential. However, genetic analysis of ERV14 deletion strains carrying thermosensitive alleles encoding for COPII components and other proteins known to participate in ER to Golgi vesicle trafficking revealed a variety ...
Small GTPases largely control membrane traffic, which is essential for the survival of all eukaryotes. Among the small GTP-binding proteins, ARF1 (ADP-ribosylation factor 1) and SAR1 (Secretion-Associated RAS super family 1) are commonly conserved among all eukaryotes with respect to both their functional and sequential characteristics. The ARF1 and SAR1 GTP-binding proteins are involved in the formation and budding of vesicles throughout plant endomembrane systems. ARF1 has been shown to play a critical role in COPI (Coat Protein Complex I)-mediated retrograde trafficking in eukaryotic systems, whereas SAR1 GTPases are involved in intracellular COPII-mediated protein trafficking from the ER to the Golgi apparatus. This review offers a summary of vesicular trafficking with an emphasis on the ARF1 and SAR1 expression patterns at early growth stages and in the de-etiolation process.
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In eukaryotic cells, the endoplasmic reticulum (ER) is a significant site of synthesis of both lipids and proteins, a lot of which should be transported to various other organelles. transfer proteins. Finally, we high light the current problems towards the field in handling the physiological legislation of COPII vesicle creation as well as the molecular information on how different cargoes, both lipids and proteins, are accommodated. likewise provides discrete ERES that are few in amount and so are apposed towards the Golgi fairly, whereas seems to absence this higher level of firm with COPII vesicles budding over the whole ER membrane [36]. Two suggested features of ERES are (i) to allow cargo destined for export to become efficiently packed and (ii) to make sure that ER resident protein and various other non-cargo substrates stay in the ER. The molecular make-up and framework of ERES can be an rising area that looks for to broaden our knowledge of the systems by which exclusive subdomains are ...
The most surprising results came when the authors examined the function of Ypt1, the Rab GTPase implicated in ER-to-Golgi transport. Vesicles prepared from a temperature-sensitive mutant in Ypt1, ypt1-3, had no defect on their ability to fuse with wild-type acceptor membranes. However, Ypt1 mutant acceptor membranes showed a dramatic defect in their ability to allow fusion with wild-type vesicles. Consistent with this the authors also find that very little Ypt1 is recruited onto vesicles when they are produced with purified COPII components, suggesting that Ypt1 normally associates with these vesicles after their initial COPII-dependent budding. However, unlike the membrane-embedded SNAREs, Ypt1 and Rabs are known to cycle on and off membranes with the assistance of a protein known as GDI. This protein has the ability to solvate the hydrophobic geranylgeranyl group at the COOH terminus of Rab proteins and extract them off the membrane which then allows them to attach to another membrane. This ...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
We explain Golgi Body with video tutorials and quizzes, using our Many Ways(TM) approach from multiple teachers.This lesson will discuss the structure and function of the golgi body.
Golgi Dynamics. How can it happen that the resident proteins appear to remain in place while the transient proteins, destined for other sites in the cell, move through the organelle in a cis to trans direction?. Over the years a number of ideas have been put forth they fall into two general models.. 1. Vesicle Transport Model. This model assumes that the cisternae are essentially stationary and contain their resident proteins. The transient proteins are selected and concentrated in vesicles by the process of vesicle formation that is driven by coat proteins and their interaction with cargo receptor proteins as described in the last lecture. See vesicle formation animation for review of how this works.. These transport vesicles bud from the periphery of the Golgi cisterna as shown in the picture above, and then fuse with the appropriate target cisterna (trans to the point of origin) via the normal vesicle targeting process. In this manner a transient protein makes is way down the Golgi stack, cis ...
The experience was fantastic. Wim Hagen was very efficient in setting up optimal data collection, while at the same time always involving us in decision-making. Wim collected a dataset for us that we used to obtain a 4.9 Å structure of the assembled COPII coat, now published in Nature Communications. This is the highest-resolution structure of a membrane-assembled coat, and one of the highest-resolution subtomogram averages obtained so far.. ...
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Intracellular transport between the ER and Golgi is mediated by vesicles that bud from donor membranes and then fuse with acceptor membranes. Bi-directional vesicle transport maintains distinct organelle composition through a process known as molecular sorting. Collectively, molecular sorting refers to the process of actively selecting or excluding proteins and lipids into transport vesicles. Some of the proteins involved in sorting have been identified although the mechanisms remain obscure. This dissertation examines proteins contained on ER-derived vesicles (Ervs) and how these proteins facilitate sorting. Erv function requires bi-directional ER to Golgi transport therefore it was determined how the cytoplamic tail sequences of Emp24p and Erv25p function in transport. Both Emp24p and Erv25p tail sequences are sufficient to direct anterograde transport and interact with COPII subunits, however the Erv25p tail is necessary to direct retrograde transport. A vexing question regarding p24 function ...
Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair (By similarity). Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes (By similarity). Involved in ER-Golgi transport (PubMed:27276012). Regulates ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby bridging together the ESCRT-III and ESCRT-I complexes (By similarity). Together with PEF1, acts as calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in ER-Golgi transport by regulating the size of COPII coats (By similarity). In response to cytosolic calcium increase, the heterodimer formed with PEF1 interacts with, and bridges together the BCR(KLHL12)
Transition zones are associated with the Golgi stacks. They are close to each other. This makes sense because the communication is more efficient. Vesicles dont need to travel long distances and the existence of the Golgi apparatus itself depends on a continuous process of vesicle incoming. It has been observed that a new transition zone led quickly to the nearby formation of a new Golgi stack. On the contrary, if a transition zone disappears, the associated Golgi cisternae are also lost. Transition zones can fuse with others and one transition zone can be split in two. Their associated Golgi stacks match this behavior. Vesicles budding from the transition zones are COPII coated vesicles ( COPII: coat protein II; Figure 1). Several proteins are involved in the formation of this COPII molecular framework: Sec16, Sar1 GTPases, Sec23/24 and Sec13/31. In this order, they are assembled at the cytosolic surface of the transition zone membranes. Transition zones are the more suitable environments for ...
The chief function of Golgi body is secretion from a cell of protein materials, such as enzymes, hormones etc., that are not easily diffusible through the cell membrane. After being synthesized in the rough endoplasmic reticulum, the secretory proteins pass into the cisternae of Golgi body through the tubules of ER and Golgi body, and are stored in the Golgi vacuoles. From the vacuoles the secretory materials are released in the cytoplasm in the form of membrane bound tiny vesicels. These vesicles then pass towards the border of the cell and fuse with the cell membrane in such a manner that the secretory materials are expelled out of the cell keeping the cell membrane unbroken. By the same mechanism the Golgi body also helps in the release of neurotransmitters and neuro-hormones from nerve cells.. ...
Résumé : ORP2 is a ubiquitously expressed OSBP-related protein previously implicated in triacylglycerol (TG) metabolism at endoplasmic reticulum (ER) - lipid droplet (LD) contacts, cholesterol transport, and adrenocortical steroidogenesis. We now characterize the functional role of ORP2 by employing ORP2-knock-out (KO) hepatoma cells generated by CRISPR-Cas9 gene editing. Loss of ORP2 did not affect the major cellular phospholipids, cholesterol, or oxysterols, nor the quantity of ER-LD contact sites. However, the knock-out resulted in reduced expression of SREBP-1 target genes and mRNAs encoding glycolytic enzymes, defective TG synthesis and storage, inhibition of LD growth upon fatty acid loading, reduction of glucose uptake, glycogen synthesis, glycolysis (ECAR) and Akt activity. ORP2 was found to form a physical complex with key controllers of Akt, Cdc37 and Hsp90. In addition to the metabolic phenotypes, the ORP2-KO cells showed defects in adhesion, lamellipodieae formation, migration and ...
The Golgi body (or Golgi complex, apparatus), and Endoplasmic reticulum (ER) are both organelles found in the majority of eukaryotic cells. They are very closely associated and show both similarities and differences in structure and function.
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... β-COP), Sec21 (γ-COP), Ret2(δ-COP), and Ret3 (ζ-COP). COPI is a coatomer that coats the vesicles transporting proteins from the ... COP1 coated vesicles also contain p24 proteins that assist with cargo sorting. COP II is a coatomer that coats the vesicles ... This complex polymerizes to form the outer layer of the coat. COP II vesicles must shed their coat before they can fuse with ... Once the vesicle is coated, it begins to travel to the ER. Before the vesicle can fuse with the ER membrane, the coats ...
"ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding protein ... Sönnichsen B, Watson R, Clausen H, Misteli T, Warren G (1996). "Sorting by COP I-coated vesicles under interphase and mitotic ... COPII vesicles Clathrin vesicles Glyceraldehyde 3-phosphate dehydrogenase#ER to Golgi transport Exomer Coat+Protein+Complex+I ... A structure of the COPI coat and the role of coat proteins in membrane vesicle assembly". Science. 349 (6244): 195-198. doi: ...
McMahon HT, Mills IG (August 2004). "COP and clathrin-coated vesicle budding: different pathways, common approaches". Curr. ... AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... and from there via small carrier vesicles to their final destination compartment. These vesicles have specific coat proteins ( ... This is an adaptor protein which helps the formation of a clathrin coat around a vesicle. This entry represents a subdomain of ...
"COP and clathrin-coated vesicle budding: different pathways, common approaches". Curr. Opin. Cell Biol. 16 (4): 379-91. doi: ... Adaptor protein (AP) complexes are found in coated vesicles and clathrin-coated pits. AP complexes connect cargo proteins and ... Clathrin coats contain both clathrin (acts as a scaffold) and adaptor complexes that link clathrin to receptors in coated ... lipids to clathrin at vesicle budding sites, as well as binding accessory proteins that regulate coat assembly and disassembly ...
COP 1 (Cytosolic coat protein complex ) : retrograde transport; Golgi ----> Endoplasmic reticulum COP 2 (Cytosolic coat protein ... As a result, vesicular transporters govern the concentration of molecules within a vesicle. Examples include: Archain ARFs ... is a membrane protein that regulates or facilitates the movement of specific molecules across a vesicle's membrane. ... each using its own coat and GTPase. ...
1991). "Beta-COP, a 110 kd protein associated with non-clathrin-coated vesicles and the Golgi complex, shows homology to beta- ... "Physical interaction of the HIV-1 Nef protein with beta-COP, a component of non-clathrin-coated vesicles essential for membrane ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Lowe M, Kreis TE (1997). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725-30. doi: ...
Activated Arf1p then recruits coat protein β-COP, a subunit of the COP-I complex, to cargo-bound receptors on the membrane. ... of SNARE proteins in the Golgi which would otherwise be bound to coat protein-coated vesicles and removed with the vesicles ... Coat protein recruitment is necessary for proper vesicle formation and transport. Brefeldin A reversibly inhibits the function ... protein transport from the endoplasmic reticulum to the golgi complex indirectly by preventing association of COP-I coat to the ...
1991). "ADP-ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: a novel role for a GTP-binding ... Eugster A, Frigerio G, Dale M, Duden R (August 2000). "COP I domains required for coatomer integrity, and novel interactions ... "Site-specific photocrosslinking to probe interactions of Arf1 with proteins involved in budding of COPI vesicles". Methods. 20 ...
Coat complexes that have been well characterized so far include coat protein-I (COP-I), COP-II, and clathrin. Clathrin coats ... Coats function to deform the donor membrane to produce a vesicle, and they also function in the selection of the vesicle cargo ... Clathrin-coated vesicles (CCVs) are found in virtually all cells and form domains of the plasma membrane termed clathrin-coated ... Coated vesicles were first purified by Barbara Pearse, who discovered the clathrin coat molecule in 1976. Caveolin proteins ...
The repertoire of COP-II paralogs available in mammals could contribute to a wide variety of COP-II coats, thus facilitating ... The COP-II complex comprises five highly conserved proteins, among these SEC31A, creating small membrane vesicles that ... Alternative splicing could further contribute to the COP-II vesicle and cargo selection diversity. CRISPR/Cas9-mediated ... the extruded membrane is separated from the ER membrane to form an intact vesicle. Most mammalian COP-II complex subunits have ...
For the membrane coated vesicle used in transport, see here. Fagol Caspase recruitment domain-containing protein 16 is an ... Lee SH, Stehlik C, Reed JC (Sep 2001). "Cop, a caspase recruitment domain-containing protein and inhibitor of caspase-1 ... 2006). "Protective role of Cop in Rip2/caspase-1/caspase-4-mediated HeLa cell death". Biochim. Biophys. Acta. 1762 (8): 742-54 ...
... clathrin-coated vesicles MeSH A11.284.430.214.190.875.190.880.180.180 - cop-coated vesicles MeSH A11.284.430.214.190.875. ... transport vesicles MeSH A11.284.430.214.190.875.190.880.180 - coated vesicles MeSH A11.284.430.214.190.875.190.880.180.160 - ... 190.880.810 - secretory vesicles MeSH A11.284.430.214.190.875.190.880.830 - synaptic vesicles MeSH A11.284.430.214.190.875. ... coated pits, cell-membrane MeSH A11.284.149.165.175.160 - caveolae MeSH A11.284.149.165.355 - glycocalyx MeSH A11.284.149.165. ...
Lowe M, Kreis TE (1997). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725-30. doi: ... a cytosolic protein complex containing subunits of non-clathrin-coated Golgi transport vesicles". Nature. 349 (6306): 248-51. ... Bermak JC, Li M, Bullock C, Weingarten P, Zhou QY (2002). "Interaction of gamma-COP with a transport motif in the D1 receptor C ... Yamasaki K, Hayashida S, Miura K, Masuzaki H, Ishimaru T, Niikawa N, Kishino T (Nov 2000). "The novel gene, gamma2-COP (COPG2 ...
COP coat proteins, the N-ethylmaleimide sensitive factor, the small transmembrane proteins of the p24 family, the p38 MAP ... "An endosomal beta COP is involved in the pH-dependent formation of transport vesicles destined for late endosomes". The Journal ... "Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle fusion in ... Gruenberg, J. E.; Howell, K. E. (1986-12-01). "Reconstitution of vesicle fusions occurring in endocytosis with a cell-free ...
Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... Eugster A, Frigerio G, Dale M, Duden R (2000). "COP I domains required for coatomer integrity, and novel interactions with ARF ... is a cytosolic protein complex that binds to dilysine motifs and reversibly associates with Golgi non-clathrin-coated vesicles ... Eugster A, Frigerio G, Dale M, Duden R (August 2000). "COP I domains required for coatomer integrity, and novel interactions ...
It is one of seven proteins in the COPI coatomer complex that coats vesicles as they bud from the Golgi complex. COPG has been ... Lowe, M; Kreis T E (November 1996). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. UNITED STATES. 271 ... Lowe M, Kreis TE (1997). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725-30. doi: ... 2000). "Duplication of genes encoding non-clathrin coat protein gamma-COP in vertebrate, insect and plant evolution". FEBS Lett ...
Chow VT, Quek HH (1997). "Alpha coat protein COPA (HEP-COP): presence of an Alu repeat in cDNA and identity of the amino ... Orcl L, Palmer DJ, Amherdt M, Rothman JE (1993). "Coated vesicle assembly in the Golgi requires only coatomer and ARF proteins ... The subunits are designated alpha-COP, beta-COP, beta-prime-COP, gamma-COP, delta-COP, epsilon-COP, and zeta-COP. The alpha-COP ... Lowe M, Kreis TE (November 1996). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725-30. ...
The Golgi coatomer complex (see MIM 601924) constitutes the coat of nonclathrin-coated vesicles and is essential for Golgi ... Lowe M, Kreis TE (November 1996). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725-30. ... Lowe M, Kreis TE (1997). "In vivo assembly of coatomer, the COP-I coat precursor". J. Biol. Chem. 271 (48): 30725-30. doi: ... Stenbeck G, Harter C, Brecht A, Herrmann D, Lottspeich F, Orci L, Wieland FT (1993). "beta'-COP, a novel subunit of coatomer". ...
Vesicle coat proteins frequently contain alpha solenoids and share common domain architecture with some NPC proteins. Three ... Field, Mark C.; Sali, Andrej; Rout, Michael P. (13 June 2011). "On a bender-BARs, ESCRTs, COPs, and finally getting your coat ... vesicle coat proteins, and nuclear pore complexes". Current Opinion in Cell Biology. 21 (1): 4-13. doi:10.1016/j.ceb.2008.12. ... and Clathrin Vesicle Coats". Cell. 142 (1): 123-132. doi:10.1016/j.cell.2010.05.030. PMC 2943847. PMID 20579721. Forwood, Jade ...
The best characterized type of vesicle is the clathrin coated vesicle (CCV). The formation of a COPII vesicle at the ... Components of COPI (cop one) a coatomer, and TSET (T-set) a membrane trafficking complex have similar heterotetramers of the AP ... but the coat of COPI is not closely related to the coats of either CCVs or COPII vesicles. AP-5 is associated with 2 proteins, ... but the ultrastructure of that coat is not known. The coat of AP-4 is unknown. An almost universal feature of coat assembly is ...
Cargo then progress toward the trans face in COPI-coated vesicles. This model proposes that COPI vesicles move in two ... ARFs are small GTPases which regulate vesicular trafficking through the binding of COPs to endosomes and the Golgi. BFA ... Proteins are delivered from the ER to the cis face using COPII-coated vesicles. ... Once matured, the TGN cisternae dissolve to become secretory vesicles. While this progression occurs, COPI vesicles continually ...
COPI-Coated Vesicles use COP-Coated Vesicles. COPII-Coated Vesicles use COP-Coated Vesicles ...
part_of COPI vesicle coat IBA Inferred from Biological aspect of Ancestor. more info ... Crystallization and preliminary X-ray analysis of the C-terminal domain of δ-COP, a medium-sized subunit of the COPI complex ... part_of COPI vesicle coat ISS Inferred from Sequence or Structural Similarity. more info ... COPI coat complex subunit delta. archain vesicle transport protein 1. coatomer delta subunit. coatomer protein complex, subunit ...
COP-COATED VESICLES. VESICULAS CUBIERTAS DE PCO. VESÍCULAS COBERTAS PELO COMPLEXO DE PROTEÍNA DO ENVOLTÓRIO. ... CLATHRIN-COATED VESICLES. VESICULAS CUBIERTAS DE CLATRINA. VESÍCULAS COBERTAS DE CLATRINA. COMMUNICABLE DISEASES, EMERGING. ... SECRETORY VESICLES. VESICULAS SECRETORAS. VESÍCULAS SECRETÓRIAS. SELF-SUSTAINED SEQUENCE REPLICATION. REPLICACION DE SECUENCIA ...
CLATHRIN-COATED VESICLES. VESÍCULAS COBERTAS DE CLATRINA. VESICULAS CUBIERTAS DE PCO. COP-COATED VESICLES. VESÍCULAS COBERTAS ... CYTOPLASMIC VESICLES. VESÍCULAS CITOPLASMÁTICAS. VESICULAS CUBIERTAS DE CLATRINA. ...
VESICLES. VESICULAS CUBIERTAS DE CLATRINA. VESÍCULAS COBERTAS PELO COMPLEXO DE PROTEÍNA DO ENVOLTÓRIO. COP-COATED VESICLES. ... CYTOPLASMIC VESICLES. VESICULAS CITOPLASMATICAS. VESÍCULAS COBERTAS DE CLATRINA. CLATHRIN-COATED ...
VESICLES. VESICULAS CUBIERTAS DE CLATRINA. VESÍCULAS COBERTAS PELO COMPLEXO DE PROTEÍNA DO ENVOLTÓRIO. COP-COATED VESICLES. ... CYTOPLASMIC VESICLES. VESICULAS CITOPLASMATICAS. VESÍCULAS COBERTAS DE CLATRINA. CLATHRIN-COATED ...
COP-COATED VESICLES. VESICULAS CUBIERTAS DE PCO. VESÍCULAS COBERTAS PELO COMPLEXO DE PROTEÍNA DO ENVOLTÓRIO. ... CLATHRIN-COATED VESICLES. VESICULAS CUBIERTAS DE CLATRINA. VESÍCULAS COBERTAS DE CLATRINA. COMMUNICABLE DISEASES, EMERGING. ... SECRETORY VESICLES. VESICULAS SECRETORAS. VESÍCULAS SECRETÓRIAS. SELF-SUSTAINED SEQUENCE REPLICATION. REPLICACION DE SECUENCIA ...
VESICLES. VESICULAS CUBIERTAS DE CLATRINA. VESÍCULAS COBERTAS PELO COMPLEXO DE PROTEÍNA DO ENVOLTÓRIO. COP-COATED VESICLES. ... CYTOPLASMIC VESICLES. VESICULAS CITOPLASMATICAS. VESÍCULAS COBERTAS DE CLATRINA. CLATHRIN-COATED ...
VESICLES. VESICULAS CUBIERTAS DE CLATRINA. VESÍCULAS COBERTAS PELO COMPLEXO DE PROTEÍNA DO ENVOLTÓRIO. COP-COATED VESICLES. ... CYTOPLASMIC VESICLES. VESICULAS CITOPLASMATICAS. VESÍCULAS COBERTAS DE CLATRINA. CLATHRIN-COATED ...
CLATHRIN-COATED VESICLES. VESÍCULAS COBERTAS DE CLATRINA. VESICULAS CUBIERTAS DE PCO. COP-COATED VESICLES. VESÍCULAS COBERTAS ... CYTOPLASMIC VESICLES. VESÍCULAS CITOPLASMÁTICAS. VESICULAS CUBIERTAS DE CLATRINA. ...
COP-COATED VESICLES. VESICULAS CUBIERTAS DE PCO. VESÍCULAS COBERTAS PELO COMPLEXO DE PROTEÍNA DO ENVOLTÓRIO. ... CLATHRIN-COATED VESICLES. VESICULAS CUBIERTAS DE CLATRINA. VESÍCULAS COBERTAS DE CLATRINA. COMMUNICABLE DISEASES, EMERGING. ... SECRETORY VESICLES. VESICULAS SECRETORAS. VESÍCULAS SECRETÓRIAS. SELF-SUSTAINED SEQUENCE REPLICATION. REPLICACION DE SECUENCIA ...
COP-COATED VESICLES. VESICULAS CUBIERTAS DE PCO. VESÍCULAS COBERTAS PELO COMPLEXO DE PROTEÍNA DO ENVOLTÓRIO. ... CLATHRIN-COATED VESICLES. VESICULAS CUBIERTAS DE CLATRINA. VESÍCULAS COBERTAS DE CLATRINA. COMMUNICABLE DISEASES, EMERGING. ... SECRETORY VESICLES. VESICULAS SECRETORAS. VESÍCULAS SECRETÓRIAS. SELF-SUSTAINED SEQUENCE REPLICATION. REPLICACION DE SECUENCIA ...
VESICLES. VESICULAS CUBIERTAS DE CLATRINA. VESÍCULAS COBERTAS PELO COMPLEXO DE PROTEÍNA DO ENVOLTÓRIO. COP-COATED VESICLES. ... CYTOPLASMIC VESICLES. VESICULAS CITOPLASMATICAS. VESÍCULAS COBERTAS DE CLATRINA. CLATHRIN-COATED ...
COP-COATED VESICLES. VESICULAS CUBIERTAS DE PCO. VESÍCULAS COBERTAS PELO COMPLEXO DE PROTEÍNA DO ENVOLTÓRIO. ... CLATHRIN-COATED VESICLES. VESICULAS CUBIERTAS DE CLATRINA. VESÍCULAS COBERTAS DE CLATRINA. COMMUNICABLE DISEASES, EMERGING. ... SECRETORY VESICLES. VESICULAS SECRETORAS. VESÍCULAS SECRETÓRIAS. SELF-SUSTAINED SEQUENCE REPLICATION. REPLICACION DE SECUENCIA ...
CLATHRIN-COATED VESICLES. VESÍCULAS COBERTAS DE CLATRINA. VESICULAS CUBIERTAS DE PCO. COP-COATED VESICLES. VESÍCULAS COBERTAS ... CYTOPLASMIC VESICLES. VESÍCULAS CITOPLASMÁTICAS. VESICULAS CUBIERTAS DE CLATRINA. ...
VESICLES. VESICULAS CUBIERTAS DE CLATRINA. VESÍCULAS COBERTAS PELO COMPLEXO DE PROTEÍNA DO ENVOLTÓRIO. COP-COATED VESICLES. ... CYTOPLASMIC VESICLES. VESICULAS CITOPLASMATICAS. VESÍCULAS COBERTAS DE CLATRINA. CLATHRIN-COATED ...
COP-COATED VESICLES. VESICULAS CUBIERTAS DE PCO. VESÍCULAS COBERTAS PELO COMPLEXO DE PROTEÍNA DO ENVOLTÓRIO. ... CLATHRIN-COATED VESICLES. VESICULAS CUBIERTAS DE CLATRINA. VESÍCULAS COBERTAS DE CLATRINA. COMMUNICABLE DISEASES, EMERGING. ... SECRETORY VESICLES. VESICULAS SECRETORAS. VESÍCULAS SECRETÓRIAS. SELF-SUSTAINED SEQUENCE REPLICATION. REPLICACION DE SECUENCIA ...
COP and clathrin-coated vesicle budding: different pathways, common approaches. . Curr Opin Cell Biol. . 2004. ;. 16. (. 4. ): ... Extracellular vesicles are derived from the multivesicular body and act in host/parasite relationships and cell-cell signaling ... Parasite extracellular vesicles: mediators of intercellular communication. . PLoS Pathog. . 2014. ;. 10. (. 8. ):. e1004289. ... Cell-cell communication between malaria-infected red blood cells via exosome-like vesicles. . Cell. . 2013. ;. 153. (. 5. ):. ...
EN] COP (coat protein) I-coated vesicles mediate intra-Golgi transport and retrograde transport from the Golgi to the ... alpha 2-COP is involved in early secretory traffic in Arabidopsis and is required for plant growth  ... These vesicles form through the action of the small GTPase ADP-ribosylation ... ... Browsing by Subject "Alpha 1-COP". RiuNet: Institutional repository of the Polithecnic University of Valencia. ...
ADP-Ribosylation factor is a subunit of the coat of Golgi-derived COP-coated vesicles: A novel role for a GTP-binding protein ... Hydrolysis of bound GTP by ARF protein triggers uncoating of Golgi-derived COP-coated vesicles ... Cytosolic ARFs are required for vesicle formation but not for cell-free intra-Golgi transport: evidence for coated vesicle- ... COPII: a membrane coat formed by Sec proteins that drive vesicle budding from the endoplasmic reticulum ...
ER to Golgi vesicle-mediated transport;C:COPI vesicle coat, CUL4 RING ubiquitin ligase complex, membrane;MFOBPA. S.X.. H.G.. ... coatomer gamma-2 subunit, putative / gamma-2 coat protein, putative / gamma-2 COP, putative. F:protein binding, clathrin ... Back to the CoP portal site. Back to the KAGIANA project homepage. ... F:protein binding, structural molecule activity, transporter activity;P:intracellular protein transport, vesicle-mediated ...
COP and clathrin-coated vesicle budding: different pathways, common approaches. Curr Opin Cell Biol. 2004;16(4):379-91. Epub ... Duden R. ER-to-Golgi transport: COP I and COP II function (Review). Mol Membr Biol. 2003;20(3):197-207. Epub 2003/08/02. doi: ...
The mammalian COPI subunits are called alpha-, beta-, beta-, gamma-, delta-, epsilon- and zeta-COP. Vesicles with COPI coats ... GO:0030126: COPI vesicle coat (Cellular component). One of two multimeric complexes that forms a membrane vesicle coat. ...
4.864154 INESSENTIAL SEC28 epsilon-COP coatomer subunit Sec28p, non-selective vesicle coating, vesicle transport, coatomer ... vesicle transport, vesicle transport, coated vesicle YKR007W 0.116917 INESSENTIAL biological_process unknown, molecular_ ... YML012W 14.541695 INESSENTIAL ERV25 vesicle coat component YLR271W 14.508198 INESSENTIAL biological_process unknown, molecular_ ... non-selective vesicle fusion*, v-SNARE, inter-Golgi transport vesicle* YHR009C -2.349478 INESSENTIAL biological_process unknown ...
COP-I) coated vesicles. Mutant COPA induces constitutive activation of stimulator of interferon genes, leading to systemic ...
Crystal structure of alpha-COP in complex with epsilon-COP provides insight into the architecture of the COPI vesicular coat. ... Schmitt HD (2010) Dsl1p/Zw10: common mechanisms behind tethering vesicles and microtubules. Trends Cell Biol 20(5):257-68 PMID ... 2009) Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex. Nat Struct Mol Biol 16( ...
COP-Coated Vesicles. * Golgi Apparatus. * Humans. * Mitosis. * Models, Biological. * Protein Transport. authors with profiles ...
ER/Golgi intermediate compartment COP, coat protein of non-clathrin-coated vesicles... ... homology β-COP, β-coat protein MAD, membrane association domain GST, glutathione S-transferase Btk, Brutons tyrosine kinase ... COP, coatomer protein ER, endoplasmic reticulum GA, Golgi apparatus GFP, green fluorescent protein VTC, vesicular-tubular ...
Phospholipase D is involved in the formation of Golgi associated clathrin coated vesicles in human parotid duct cells ... HIV-1 Nef targets MHC-I and CD4 for degradation via a final common beta-COP-dependent pathway in T cells ... that induces the endocytosis of CD4 mediated by clathrin-coated vesicles (CCVs) (Burtey et al., 2007; Greenberg et al., 1997). ... Shedding of ciliary vesicles at a glance. Check out our latest Cell Science at a Glance article and accompanying poster for an ...
  • EN] COP (coat protein) I-coated vesicles mediate intra-Golgi transport and retrograde transport from the Golgi to the endoplasmic reticulum. (upv.es)
  • Vesicles with COPI coats are found associated with Golgi membranes at steady state. (ntu.edu.sg)
  • W. E. ( I 998) Trends Received 2 March 2000 0 2000 Biochemical Society 512 green fluorescent protein mutagenesis, Sar1 COP, coatomer protein ER , endoplasmic reticulum GA, Golgi apparatus GFP, green fluorescent protein VTC, vesicular-tubular clusters or intermediate. (silverchair.com)
  • Because both Arf and PLD1 stimulate vesicle formation in the Golgi, these data raise the possibility that vesicle formation and trafficking may play a role in the transduction of intracellular signals. (embl.de)
  • Crystallization and preliminary X-ray analysis of the C-terminal domain of δ-COP, a medium-sized subunit of the COPI complex involved in membrane trafficking. (nih.gov)
  • Hsia KC and Hoelz A (2010) Crystal structure of alpha-COP in complex with epsilon-COP provides insight into the architecture of the COPI vesicular coat. (yeastgenome.org)
  • One of two multimeric complexes that forms a membrane vesicle coat. (ntu.edu.sg)
  • Activation of phospholipase D1 (PLD1) by Arf has been implicated in vesicle transport and membrane trafficking. (embl.de)
  • Transient N-glycosylation abnormalities likely due to a de novo loss-of-function mutation in the delta subunit of coat protein I. Reunert J, et al . (nih.gov)
  • Structural characterization of Tip20p and Dsl1p, subunits of the Dsl1p vesicle tethering complex. (yeastgenome.org)
  • That such enzymes are formed in the protoplasm is evident from the behaviour of hyphae, which have been observed to pierce cell-membranes, the chitinous coats of insects, artificial collodion films and layers of wax, &c. (yourdictionary.com)
  • It has similarities to heat shock proteins and clathrin-associated proteins, and may be involved in vesicle structure or trafficking. (nih.gov)
  • The role of coat proteins in the biosynthesis of secretory proteins. (wikidata.org)
  • Equally, how can viral researchers know that they are not detecting similarly sized non-viral vesicles or empty vectors during vaccine production? (viroliegy.com)
  • ACG is one of the largest manufacturer of empty hard capsules in the world, offering a complete range of solutions beginning with empty capsules, granulation and coating, capsule filling, tabletting, packaging films, blister packing and carton packing, to end-of-line solutions. (ondrugdelivery.com)
  • Herein, a zeolitic imidazolate framework derived amorphous CoP combined with carbon nanotubes conductive network composites ([email protected]) has been synthesized as an effective dual-electrocatalyst for accelerating the redox kinetics of polysulfides to prolong the lifespan of Li-S batteries. (energymaterj.com)
  • How cells unify and organize the curvature-generating factors at the nanoscale is presented for three ubiquitous coats central for membrane trafficking in eukaryotes: clathrin-coated pits, caveolae, and COPI and COPII coats. (nature.com)
  • The Sar1 family of proteins initiates the intracellular transport of proteins in COPII (coat protein)-coated vesicles. (nih.gov)
  • Our data suggest that chylomicrons, which vastly exceed the size of typical COPII vesicles, are selectively recruited by the COPII machinery for transport through the secretory pathways of the cell. (nih.gov)
  • COPII coat assembly and selective export from the endoplasmic reticulum. (nih.gov)
  • A structural view of the COPII vesicle coat. (nih.gov)
  • The outer surface of these vesicles is covered with a lattice-like network of COP (coat protein complex) proteins, either COPI or COPII. (nih.gov)
  • COPI coated vesicles transport backwards from the cisternae of the GOLGI APPARATUS to the rough endoplasmic reticulum ( ENDOPLASMIC RETICULUM, ROUGH ), while COPII coated vesicles transport forward from the rough endoplasmic reticulum to the Golgi apparatus. (nih.gov)
  • This process is mediated by the coat protein complex II (COPII) machinery, which at the minimum, comprises the Sar1 GTPase and the cytosolic protein complexes Sec23/Sec24 (Sec23/24) and Sec13/Sec31 (Sec13/31). (scripps.edu)
  • We after that asked if the COPII vesicle program that mediates trafficking in the ER towards the Golgi includes a function in Golgi biogenesis. (angiogenesis-blog.com)
  • We propose that the integration of individual mechanisms into a highly controlled, robust process of curvature generation often relies on the assembly of proteins into coats. (nature.com)
  • Symmetrical arrangement of proteins under release-ready vesicles in presynaptic terminals. (academictree.org)
  • This traffic is bidirectional, to ensure that proteins required to form vesicles are recycled. (embl.de)
  • Activated small guanine triphosphatases (GTPases) attract coat proteins to specific membrane export sites, thereby linking coatomers to export cargos. (embl.de)
  • As coat proteins polymerise, vesicles are formed and budded from membrane-bound organelles. (embl.de)
  • A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. (lookformedical.com)
  • Some portray biological membranes as molecular putty readily fashioned into different shapes (vesicles, tubes, and sheets) by proteins or protein complexes. (nih.gov)
  • These proteins, called ADP-ribosylation factors, or Arfs, have recently been found to 1) interact with specific lipid components of membranes, 2) modify the lipid composition and release potential second messengers through activation of phospholipase D (PLD), and 3) regulate the assembly of at least a subset of protein complexes or membrane coats (for reviews, see refs. (nih.gov)
  • AP complexes connect cargo proteins and lipids to clathrin at vesicle budding sites, as well as binding accessory proteins that regulate coat assembly and disassembly (such as AP180, epsins and auxilin). (xfam.org)
  • Membrane traffic along the eukaryotic secretory pathway starts with the selective packing of biosynthetic cargo into nascent vesicles that are forming on the endoplasmic reticulum (ER). (scripps.edu)
  • TRANSPORT VESICLES formed when cell-membrane coated pits ( COATED PITS, CELL-MEMBRANE ) invaginate and pinch off. (nih.gov)
  • An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE. (lookformedical.com)
  • AP (adaptor protein) complexes are found in coated vesicles and clathrin-coated pits. (xfam.org)
  • This review highlights advances in magnetic labeling of both cells and extracellular vesicles, which is one of the hottest branches in biology. (freewechat.com)
  • Clathrin coats contain both clathrin (acts as a scaffold) and adaptor complexes that link clathrin to receptors in coated vesicles. (xfam.org)
  • The main structural coat protein of COATED VESICLES which play a key role in the intracellular transport between membranous organelles. (lookformedical.com)
  • The emerging theme is that these coats arrange and coordinate curvature-generating factors in time and space to dynamically shape membranes to accomplish membrane trafficking within cells. (nature.com)
  • Using similar examples and Mary, Seat writing services you havent on the power of persons of to be and value skill, you pinch off and who vesicle, and. (lsp-poltekapp.org)
  • The zeta subunit may be involved in regulating the coat assembly and, hence, the rate of biosynthetic protein transport due to its association-dissociation properties with the coatomer complex (By similarity). (nih.gov)
  • Dsl1p/Zw10: common mechanisms behind tethering vesicles and microtubules. (mpg.de)
  • A tethering complex recruits SNAREs and grabs vesicles. (mpg.de)
  • FRAP evaluation revealed which the mEGFPCTb-COP indication recovered quickly in uninduced cells (= 15 for (C) TbArf1-3Tcon1 [Q71L], = 11 for (+) TbArf1-3Tcon1 [Q71L]. (angiogenesis-blog.com)
  • Vesicle capture by membrane-bound Munc13-1 requires self-assembly into discrete clusters. (academictree.org)
  • Evaluation from the inhibitory information shows that in early endosomes and endocytic vesicles NHE3 can be of main importance, whereas plasma membrane NHE3 takes on a minor part. (thetechnoant.info)
  • A link between ER tethering and COP-I vesicle uncoating. (mpg.de)
  • Analysis of the inhibitory profiles indicates that in early endosomes and endocytic vesicles NHE3 is usually of major importance, whereas plasma VX-745 membrane NHE3 plays a minor role. (ncbedbugs.com)