Clathrin Heavy Chains: The heavy chain subunits of clathrin.Clathrin: 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.Clathrin Light Chains: The light chain subunits of clathrin.Clathrin-Coated Vesicles: 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.Endocytosis: Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.Coated Pits, Cell-Membrane: 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.Myosin Heavy Chains: The larger subunits of MYOSINS. The heavy chains have a molecular weight of about 230 kDa and each heavy chain is usually associated with a dissimilar pair of MYOSIN LIGHT CHAINS. The heavy chains possess actin-binding and ATPase activity.Auxilins: A family of proteins that play a role as cofactors in the process of CLATHRIN recycling in cells.Adaptor Protein Complex 2: An adaptor protein complex primarily involved in the formation of clathrin-related endocytotic vesicles (ENDOSOMES) at the CELL MEMBRANE.Adaptor Proteins, Vesicular Transport: 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.Immunoglobulin Heavy Chains: The largest of polypeptide chains comprising immunoglobulins. They contain 450 to 600 amino acid residues per chain, and have molecular weights of 51-72 kDa.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.Monomeric Clathrin Assembly Proteins: A subclass of clathrin assembly proteins that occur as monomers.Adaptor Protein Complex alpha Subunits: 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.Dynamins: 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.Adaptor Protein Complex 1: A clathrin adaptor protein complex primarily involved in clathrin-related transport at the TRANS-GOLGI NETWORK.trans-Golgi Network: A network of membrane compartments, located at the cytoplasmic side of the GOLGI APPARATUS, where proteins and lipids are sorted for transport to various locations in the cell or cell membrane.Adaptor Protein Complex beta Subunits: A family of large adaptin protein complex subunits of approximately 90-130 kDa in size.Endosomes: Cytoplasmic vesicles formed when COATED VESICLES shed their CLATHRIN coat. Endosomes internalize macromolecules bound by receptors on the cell surface.Molecular Sequence Data: 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.Amino Acid Sequence: 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.Protein Transport: 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.Chlorpromazine: The prototypical phenothiazine antipsychotic drug. Like the other drugs in this class chlorpromazine's antipsychotic actions are thought to be due to long-term adaptation by the brain to blocking DOPAMINE RECEPTORS. Chlorpromazine has several other actions and therapeutic uses, including as an antiemetic and in the treatment of intractable hiccup.Pinocytosis: The engulfing of liquids by cells by a process of invagination and closure of the cell membrane to form fluid-filled vacuoles.Golgi Apparatus: 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)Protein Binding: 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.Vesicular Transport Proteins: 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.Heavy Chain Disease: A disorder of immunoglobulin synthesis in which large quantities of abnormal heavy chains are excreted in the urine. The amino acid sequences of the N-(amino-) terminal regions of these chains are normal, but they have a deletion extending from part of the variable domain through the first domain of the constant region, so that they cannot form cross-links to the light chains. The defect arises through faulty coupling of the variable (V) and constant (C) region genes.Myosins: A diverse superfamily of proteins that function as translocating proteins. They share the common characteristics of being able to bind ACTINS and hydrolyze MgATP. Myosins generally consist of heavy chains which are involved in locomotion, and light chains which are involved in regulation. Within the structure of myosin heavy chain are three domains: the head, the neck and the tail. The head region of the heavy chain contains the actin binding domain and MgATPase domain which provides energy for locomotion. The neck region is involved in binding the light-chains. The tail region provides the anchoring point that maintains the position of the heavy chain. The superfamily of myosins is organized into structural classes based upon the type and arrangement of the subunits they contain.Macromolecular Substances: 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.Base Sequence: The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.Vacuoles: Any spaces or cavities within a cell. They may function in digestion, storage, secretion, or excretion.Cell Line: Established cell cultures that have the potential to propagate indefinitely.Mutation: 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.Transferrin: 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.Cattle: 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.Recombinant Fusion Proteins: 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.Cell Membrane: The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.HeLa Cells: 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.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.Gene Rearrangement, B-Lymphocyte, Heavy Chain: Ordered rearrangement of B-lymphocyte variable gene regions of the IMMUNOGLOBULIN HEAVY CHAINS, thereby contributing to antibody diversity. It occurs during the first stage of differentiation of the IMMATURE B-LYMPHOCYTES.Microscopy, Electron: 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.Protein Structure, Tertiary: 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.Microscopy, Fluorescence: 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.Polymerase Chain Reaction: In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.Immunoglobulin Light Chains: Polypeptide chains, consisting of 211 to 217 amino acid residues and having a molecular weight of approximately 22 kDa. There are two major types of light chains, kappa and lambda. Two Ig light chains and two Ig heavy chains (IMMUNOGLOBULIN HEAVY CHAINS) make one immunoglobulin molecule.Biological Transport: 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.Sequence Homology, Amino Acid: The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.Carrier Proteins: Transport proteins that carry specific substances in the blood or across cell membranes.Salicylic Acid: A compound obtained from the bark of the white willow and wintergreen leaves. It has bacteriostatic, fungicidal, and keratolytic actions.Prokaryotic Initiation Factor-1: The smallest of the three prokaryotic initiation factors with a molecular size of approximately 8 kD. It binds near the A-site of the 30S subunit of RIBOSOMES and may play a role in preventing premature addition of aminoacyl-tRNA-linked PEPTIDE ELONGATION FACTOR TU to the ribosome during the initiation of a peptide chain (PEPTIDE CHAIN INITIATION, TRANSLATIONAL).Abscisic Acid: Abscission-accelerating plant growth substance isolated from young cotton fruit, leaves of sycamore, birch, and other plants, and from potatoes, lemons, avocados, and other fruits.

Functional organization of clathrin in coats: combining electron cryomicroscopy and X-ray crystallography. (1/110)

The sorting of specific proteins into clathrin-coated pits and the mechanics of membrane invagination are determined by assembly of the clathrin lattice. Recent structures of a six-fold barrel clathrin coat at 21 A resolution by electron cryomicroscopy and of the clathrin terminal domain and linker at 2.6 A by X-ray crystallography together show how domains of clathrin interact and orient within the coat and reveal the strongly puckered shape and conformational variability of individual triskelions. The beta propeller of the terminal domain faces the membrane so that recognition segments from adaptor proteins can extend along its lateral grooves. Clathrin legs adapt to different coat environments in the barrel by flexing along a segment at the knee that is free of contacts with other molecules.  (+info)

ADP-ribosylation factor 6 and endocytosis at the apical surface of Madin-Darby canine kidney cells. (2/110)

We report that the small GTPase, ADP-ribosylation factor 6 (ARF6), is present only on the apical surface of polarized MDCK epithelial cells. Overexpression of a mutant of ARF6, ARF6-Q67L, which is predicted to be in the GTP-bound form, stimulates endocytosis exclusively at this surface. Surprisingly, overexpression of the mutant ARF6-T27N, which is predicted to be in the GDP-bound form, also stimulated apical endocytosis, though to a lesser extent. ARF6-stimulated endocytosis is inhibited by a dominant-negative form of dynamin, or a dominant-negative hub fragment of clathrin heavy chain, indicating that it is mediated by clathrin. Correspondingly, overexpression of either mutant of ARF6 leads to an increase in the number of clathrin-coated pits at the apical plasma membrane. When ARF6-Q67L is overexpressed in the presence of the dominant-negative dynamin, the ARF6-Q67L colocalizes with clathrin and with IgA bound to its receptor. We conclude that ARF6 is an important modulator of clathrin-mediated endocytosis at the apical surface of epithelial cells.  (+info)

Human monocyte activation by cleaved form of alpha-1-antitrypsin involvement of the phagocytic pathway. (3/110)

Production of alpha-1-antitrypsin (AAT) by human monocytes is an important factor in controlling tissue damage by proteases in the microenvironment of inflammation. Increases, of four- to eightfold, in numbers of macrophages and levels of AAT and its cleavage fragments have been found in various inflammatory loci. We have found that the C-terminal peptide (C-36) of AAT, produced by specific proteinase cleavage when added in its fibrillar form at concentrations >/=5 microM to monocytes in culture for 24 h, significantly increases low density lipoprotein (LDL) binding and uptake, up-regulates levels of LDL receptors and also induces proinflammatory cytokine (interleukin-1, interleukin-6 and tumour necrosis factor alpha) production and glutathione reductase activity. Because it is known that various cells selectively internalize surface receptors and their ligands through receptor-mediated endocytosis via clathrin-coated pits, we tested whether antibodies raised against the clathrin heavy chain would block the effects of the fibrillar form of C-36 on human monocytes in culture. Addition of excess anti-(clathrin HC) with 10 microM fibrillar C-36 diminished the stimulatory effects of the latter on LDL binding, uptake and LDL receptor levels. In contrast, however, in the presence of anti-(clathrin HC), the potentially cytotoxic effects of fibrils, such as induction of cytokines, free radicals and cytosolic activity of cathepsin D, were much greater than those observed when cells were treated with fibrils alone. These results suggest that endocytosis is the pathway by which C-36 fibrils upregulate LDL receptors, and may be the natural mechanism for fibril clearance. We infer that human monocytes clear C-36 fibrils by a clathrin-dependent pathway, presumably endocytotic, and that loss of this pathway amplifies the cytotoxic effects of the fibrils by increasing their availability to other specific or nonspecific sites through which they exert their cytotoxic effects.  (+info)

Role for Drs2p, a P-type ATPase and potential aminophospholipid translocase, in yeast late Golgi function. (4/110)

ADP-ribosylation factor appears to regulate the budding of both COPI and clathrin-coated transport vesicles from Golgi membranes. An arf1Delta synthetic lethal screen identified SWA3/DRS2, which encodes an integral membrane P-type ATPase and potential aminophospholipid translocase (or flippase). The drs2 null allele is also synthetically lethal with clathrin heavy chain (chc1) temperature-sensitive alleles, but not with mutations in COPI subunits or other SEC genes tested. Consistent with these genetic analyses, we found that the drs2Delta mutant exhibits late Golgi defects that may result from a loss of clathrin function at this compartment. These include a defect in the Kex2-dependent processing of pro-alpha-factor and the accumulation of abnormal Golgi cisternae. Moreover, we observed a marked reduction in clathrin-coated vesicles that can be isolated from the drs2Delta cells. Subcellular fractionation and immunofluorescence analysis indicate that Drs2p localizes to late Golgi membranes containing Kex2p. These observations indicate a novel role for a P-type ATPase in late Golgi function and suggest a possible link between membrane asymmetry and clathrin function at the Golgi complex.  (+info)

Spatially regulated recruitment of clathrin to the plasma membrane during capping and cell translocation. (5/110)

Clathrin-coated vesicles bud from selected cellular membranes to traffic-specific intracellular proteins. To study the dynamic properties of clathrin-coated membranes, we expressed clathrin heavy chain tagged with green fluorescent protein (GFP) in Dictyostelium cells. GFP-clathrin was functional and retained the native properties of clathrin: the chimeric protein formed classic clathrin lattices on cellular membranes and also rescued phenotypic defects of clathrin null cells. GFP-clathrin distributed into punctate loci found throughout the cytoplasm, on the plasma membrane, and concentrated to a perinuclear location. These clathrin-coated structures were remarkably motile and capable of rapid and bidirectional transport across the cell. We identified two local domains of the plasma membrane as sites for clathrin recruitment in motile cells. First, as cells translocated or changed shape and retracted their tails, clathrin was transiently concentrated on the membrane at the back of the cell tail. Second, as cells capped their cell surface receptors, clathrin was recruited locally to the membrane under the tight cap of cross-linked receptors. This suggests that local sites for clathrin polymerization on specific domains of the plasma membrane undergo rapid and dynamic regulation in motile cells.  (+info)

Clathrin heavy chain, light chain interactions. (6/110)

Purified pig brain clathrin can be reversibly dissociated and separated into heavy chain trimers and light chains in the presence of non-denaturing concentrations of the chaotrope thiocyanate. The isolated heavy chain trimers reassemble into regular polygonal cage structures in the absence of light chains. The light chain fraction can be further resolved into its two components L alpha and L beta which give different one-dimensional peptide maps. Radiolabelled light chains bind with high affinity (KD < 10(-10) M) to heavy chain trimers, to heavy chain cages and to a 110,000 mol. wt. tryptic fragment of the heavy chain. Both light chains compete with each other and with light chains from other sources for the same binding sites on heavy chains and c.d. spectroscopy shows that the two pig brain light chains possess very similar structures. We conclude that light chains from different sources, despite some heterogeneity, have a highly conserved, high affinity binding site on the heavy chain but are not essential for the formation of regular cage structures.  (+info)

Biochemical and immunological studies on clathrin light chains and their binding sites on clathrin triskelions. (7/110)

Clathrin light chains from bovine brain tissue (LC alpha and LC beta) are monomeric proteins with an average mol. wt. of approximately 33,000, as determined by sedimentation equilibrium. Solution studies on purified light chains indicate a large Stokes radius (Re = 3.3 nm) and little defined secondary structure. Both light chains bind specifically and with high affinity (KA approximately 5 x 10(7)/M) to overlapping sites on clathrin heavy chains. These binding sites are contained within a 125,000 dalton heavy chain fragment that forms truncated triskelions with legs, 15 nm shorter than those of intact triskelions. As judged by immuno-electron microscopy, light chain-specific IgG molecules bind mostly to the center of triskelions, but there are also sites that are scattered some 16 nm along the proximal part of triskelion legs. From heterologous binding experiments using human placenta light chains and heavy chain fragments from bovine brain clathrin, it is concluded that the domains of light and heavy chains that are involved in the interaction are conserved across tissue and species boundaries.  (+info)

NGF signals through TrkA to increase clathrin at the plasma membrane and enhance clathrin-mediated membrane trafficking. (8/110)

Neurotrophin (NT) signals may be moved from axon terminals to neuron cell bodies via signaling endosomes-organelles in which NTs continue to be bound to their activated receptors. Suggesting that clathrin-coated membranes serve as one source of signaling endosomes, in earlier studies we showed that nerve growth factor (NGF) treatment increased clathrin at the plasma membrane and resulted in colocalization of clathrin with TrkA, the receptor tyrosine kinase for NGF. Strikingly, however, we also noted that most clathrin puncta at the surface of NGF-treated cells did not colocalize with TrkA, raising the possibility that NGF induces a general increase in clathrin-coated membrane formation. To explore this possibility further, we examined the distribution of clathrin in NGF- and BDNF-treated cells. NGF signaling in PC12 cells robustly redistributed the adaptor protein AP2 and the clathrin heavy chain (CHC) to surface membranes. Using confocal and epifluorescence microscopy, as well as biochemical assays, we showed the redistribution of clathrin to be attributable to the activation of TrkA. Significantly, NGF signaled through TrkA to induce an increase in clathrin-mediated membrane trafficking, as revealed in the increased endocytosis of transferrin. In that BDNF treatment increased AP2 and clathrin at the surface membranes of hippocampal neurons, these findings may represent a physiologically significant response to NTs. We conclude that NT signaling increases clathrin-coated membrane formation and clathrin-mediated membrane trafficking and speculate that this effect contributes to their trophic actions via the increased internalization of receptors and other proteins that are present in clathrin-coated membranes.  (+info)

*Vinculin

Fausser JL, Ungewickell E, Ruch JV, Lesot H (1994). "Interaction of vinculin with the clathrin heavy chain". J. Biochem. 114 (4 ...

*CLTB

Clathrin is a large, soluble protein composed of heavy and light chains. It functions as the main structural component of the ... Clathrin, light chain B is a protein in humans that is encoded by the CLTB gene. ... This gene encodes one of two clathrin light chain proteins which are believed to function as regulatory elements. Alternative ...

*STX10

Esk C, Chen CY, Johannes L, Brodsky FM (January 2010). "The clathrin heavy chain isoform CHC22 functions in a novel endosomal ...

*CLTC

"Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3". J. Biol. Chem ... Clathrin heavy chain 1 is a protein that in humans is encoded by the CLTC gene. Clathrin is a major protein component of the ... "Entrez Gene: CLTC clathrin, heavy chain (Hc)". Tebar, F; Bohlander S K; Sorkin A (Aug 1999). "Clathrin assembly lymphoid ... The basic subunit of the clathrin coat is composed of three heavy chains and three light chains. CLTC has been shown to ...

*CLINT1

The CLINT1 protein binds to the terminal domain of the clathrin heavy chain and stimulates clathrin cage vesicle assembly. ... Clathrin interactor 1 (CLINT1), also known as EPSIN4, is a protein which in humans is encoded by the CLINT1 gene. ... Clathrin coated vesicles enable neurotransmitter receptors and other proteins to be endocytosed or taken up across neuronal ... 2004). "Clathrin adaptor epsinR is required for retrograde sorting on early endosomal membranes". Dev. Cell. 6 (4): 525-38. doi ...

*Epsin

... in higher eukaryotes there are several conserved motifs such as the clathrin-binding motifs which bind clathrin heavy chain, ... The epsin homologue of C. elegans is EPN-1. EPN-1 conserves the UIM, ENTH domain, and clathrin-binding motif. ... Chen X, Irani NG, Firml, J (2011). "Clathrin - mediated endocytosis: the gateway into plant cells". Current Opinion in Plant ... Epsin 4, which encodes the protein enthoprotin, now known as clathrin interactor 1 (CLINT1), has been shown to be involved in ...

*Clathrin

The clathrin triskelion is composed of three clathrin heavy chains interacting at their C-termini, each ~190 kDa heavy chain ... The main clathrin heavy chain, located on chromosome 17 in humans, is found in all cells. A second clathrin heavy chain gene, ... The three heavy chains provide the structural backbone of the clathrin lattice, and the three light chains are thought to ... It forms a triskelion shape composed of three clathrin heavy chains and three light chains. When the triskelia interact they ...

*Diffuse large B-cell lymphoma

HLA-B encodes a heavy chain of HLA class I, that heterodimerizes with a light chain. The HLA class I has a central role in the ... It is a coactivator for steroid hormones, and the synthesized protein is involved in clathrin-mediated endocytosis. But the ...

*List of MeSH codes (D12.776.543)

... clathrin heavy chains MeSH D12.776.543.990.200.750 -- clathrin light chains MeSH D12.776.543.990.300.150 -- ADP-ribosylation ... cd98 heavy chain MeSH D12.776.543.585.200.374.750.500.500 -- antigens, cd98 light chains MeSH D12.776.543.585.200.500 -- amino ... cd98 heavy chain MeSH D12.776.543.585.200.500.500.500.500 -- antigens, cd98 light chains MeSH D12.776.543.585.200.500.500.500. ... integrin beta chains MeSH D12.776.543.750.705.408.200.249 -- antigens, cd18 MeSH D12.776.543.750.705.408.200.500 -- antigens, ...

*DNAH1

Dynein axonemal heavy chain 1 is a protein that in humans is encoded by the DNAH1 gene. This gene encodes an inner dynein arm ... Skånland SS, Wälchli S, Brech A, Sandvig K (2009). "SNX4 in complex with clathrin and dynein: implications for endosome ... Dynein axonemal heavy chain 1". Retrieved 2017-11-06. Zuccarello D, Ferlin A, Cazzadore C, Pepe A, Garolla A, Moretti A, ... which encodes an inner arm heavy chain dynein, lead to male infertility from multiple morphological abnormalities of the sperm ...

*Endocytosis

The main scaffold component of clathrin coat is the 190-kD protein called clathrin heavy chain (CHC), which is associated with ... Clathrin-coated vesicles (CCVs) are found in virtually all cells and form domains of the plasma membrane termed clathrin-coated ... Coat complexes that have been well characterized so far include coat protein-I (COP-I), COP-II, and clathrin. Clathrin coats ... kD protein called clathrin light chain (CLC), forming three-legged trimers called triskelions. Vesicles selectively concentrate ...

*Housekeeping gene

FTH1 Heavy chain of Ferritin GDI2 rab/ras vessicular trafficking GUK1 Guanylate kinase transfers phosphate from ATP to GMP HPRT ... 018229 ANXA6 Annexin 6 ANXA7 Annexin 7 AP1B1 Coated vessicles CLTA Clathrin A (vessicles) CLTB Clathrin B (vessicles) CLTC MTX2 ... mitochondrial respiratory chain complex III or cytochrome b-c1 complex) UQCR10 NM_013387 UQCR11 NM_006830 Homo sapiens ... that is involved in complex II of the mitochondrial electron transport chain and is responsible for transferring electrons from ...

*MAP1A

... polypeptide that presumably undergoes proteolytic processing to generate the final MAP1A heavy chain and LC2 light chain. ... "Interactions between adaptor protein-1 of the clathrin coat and microtubules via type 1a microtubule-associated proteins". J. ... Mann SS, Hammarback JA (1994). "Molecular characterization of light chain 3. A microtubule binding subunit of MAP1A and MAP1B ... light chains determine distinct functional properties". J. Neurosci. 22 (6): 2106-14. PMID 11896150. Ikeda A, Zheng QY, Zuberi ...

*SNARE (protein)

... is composed of a heavy chain (100KDa) and a light chain (50kDa) connected by a disulfide bond. The heavy chain is responsible ... clathrin-coated, single-membrane vesicles containing Atg16L, the v-SNARE VAMP7, and its partner t-SNAREs: Syntaxin-7, Syntaxin- ... The light chain is released from the heavy chain by the reduction of the disulfide bond holding the two together. The reduction ... The heavy chain undergoes a conformational change important for translocating the light chain into the cytosol of the neuron. ...

*Transferrin

clathrin-coated pit. • secretory granule lumen. • endosome membrane. • extracellular exosome. • extracellular space. • clathrin ... In humans, transferrin consists of a polypeptide chain containing 679 amino acids and two carbohydrate chains. The protein is ... Carbohydrate deficient transferrin increases in the blood with heavy ethanol consumption and can be monitored through ...

*Laboratory of Molecular Biology

Barbara Pearse discovered the major components of clathrin-coated vesicles, structures formed during endocytosis, and a low ... J. A. Steitz, (1969) "Polypetide Chain Initiation: Nucleotide Sequences of the Three Ribosomal Binding Sites in Bacteriophage ... be solved by X-ray analysis using a heavy metal atom labeling technique. Hugh Huxley discovered that muscle contraction works ...
Clathrin, a three-legged triskelion composed of three clathrin heavy chains (CHCs) and three light chains (CLCs), plays a critical role in clathrin-mediated endocytosis (CME) in eukaryotic cells. In this study, the genes ZmCHC1 and ZmCHC2 encoding clathrin heavy chain in maize were cloned and characterized for the first time in monocots. ZmCHC1 encodes a 1693-amino acid-protein including 29 exons and 28 introns, and ZmCHC2 encodes a 1746-amino acid-protein including 28 exons and 27 introns. The high similarities of gene structure, protein sequences and 3D models among ZmCHC1, and Arabidopsis AtCHC1 and AtCHC2 suggest their similar functions in CME. ZmCHC1 gene is predominantly expressed in maize roots instead of ubiquitous expression of ZmCHC2. Consistent with a typical predicted salicylic acid (SA)-responsive element and four predicted ABA-responsive elements (ABREs) in the promoter sequence of ZmCHC1, the expression of ZmCHC1 instead of ZmCHC2 in maize roots is significantly up-regulated by SA or ABA,
In this report we have addressed the biological consequence of endofin-mediated TOM1 recruitment onto endosomes. Our results collectively suggest that TOM1 serves as an adaptor for endofin to recruit clathrin heavy chain onto the endosomes. This conclusion is supported by several lines of evidence as described in our study.. First, via large-scale pull-down experiments using immobilized GST-TOM1(300-492), we have recovered clathrin heavy chain as the major and specific partner for TOM1. This conclusion was corroborated by analytical pull-down experiments showing that clathrin heavy chain was very efficiently retained by immobilized GST-TOM1(300-492), so much so that it was depleted from the cytosol. The specific interaction between TOM1 and clathrin heavy chain was further defined by our identification of three sites in the carboxyl-terminal region of TOM1, which seem to act together for efficient interaction with clathrin. Moreover, the specific blockage of interaction between TOM1 and clathrin ...
Clathrin-coated vesicles are the most prominent carriers of membrane traffic from cell surface to endosomes (endocytosis), a pathway by which hormones, transferrin, immunoglobulins, LDL, viruses, and their receptors enter cells. They are also important for traffic between endosomes and the trans-Golgi network. In this presentation, I will discuss (i) technological and analytical advances that I developed to directly visualize clathrin-mediated membrane traffic in three dimensions and in living cells; (ii) data obtained using these advances that defined a role for actin filament polymerization in counteracting membrane tension during clathrin-coated vesicle budding at the apical surface of polarized epithelial cells; and (iii) how these advances can be used to study a wide variety of biological processes that occur in living cells and tissues. ...
Bicaudal-D (Bic-D), Egalitarian (Egl), microtubules and their motors form a transport machinery that localizes a remarkable diversity of mRNAs to specific cellular regions during oogenesis and embryogenesis. Bic-D family proteins also promote dynein-dependent transport of Golgi vesicles, lipid droplets, synaptic vesicles and nuclei. However, the transport of these different cargoes is still poorly understood. We searched for novel proteins that either mediate Bic-D-dependent transport processes or are transported by them. Clathrin heavy chain (Chc) co-immunopurifies with Bic-D in embryos and ovaries, and a fraction of Chc colocalizes with Bic-D. Both proteins control posterior patterning of the Drosophila oocyte and endocytosis. Although the role of Chc in endocytosis is well established, our results show that Bic-D is also needed for the elevated endocytic activity at the posterior of the oocyte. Apart from affecting endocytosis indirectly by its role in osk mRNA localization, Bic-D is also ...
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BACKGROUND: Clathrin is a multimeric protein involved in vesicle coat assembly. Recently clathrin distribution was reported to change during the cell cycle and was found to associate with the mitotic spindle. Here we test whether the recruitment of clathrin to the spindle is indicative of a critical functional contribution to mitosis. METHODOLOGY/PRINCIPAL FINDINGS: Previously a chicken pre-B lymphoma cell line (DKO-R) was developed in which the endogenous clathrin heavy chain alleles were replaced with the human clathrin heavy chain under the control of a tetracycline-regulatable promoter. Receptor-mediated and fluid-phase endocytosis were significantly inhibited in this line following clathrin knockout, and we used this to explore the significance of clathrin heavy chain expression for cell cycle progression. We confirmed using confocal microscopy that clathrin colocalised with tubulin at mitotic spindles. Using a propidium iodide flow cytometric assay we found no statistical difference in the cell
The kinetics of CHC phosphorylation in activated T cells was slow compared with the total protein tyrosine phosphorylation in cell lysates (not depicted). This delay suggested that other signaling events are initiated before CHC phosphorylation. We had previously found that the activation of c-Src kinase or Lyn kinase, a Src kinase family member, was required for CHC phosphorylation after EGFR and BCR stimulation, respectively (20, 21). To address whether the activity of a Src family kinase was necessary for CHC phosphorylation in activated T cells, we treated Jurkat cells with various concentrations of the Src family kinase inhibitor PP1 before stimulation with soluble anti-CD3 Ab. At increasing concentrations of PP1, but not the serine/threonine kinase inhibitor H7, the level of inducible CHC phosphorylation was diminished (Fig. 2 A). Additionally, in the presence of PP1, the basal level of CHC phosphorylation in Jurkat cells before the induction of TCR internalization was also decreased, ...
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The structure of Clathrin is known as a triskeleion structure with there being three bent legs extending from a central point known as the central trimerization domain. Clathrin is made up of six chains of protein that are braided together in such a way to form to form its distinct shape. Three of these chains are known as heavy chains and form the backbone of Clathrin, they consist of two sub domains a N-terminal zone and a proximal leg domain. A seven bladed β-propeller structure is what the N-terminal domain consists off. While the proximal leg consists of a super Helix (Conner and Schmid, 2002). The other three chains are known as light chains and regulate formation and disassembly of the Clathrin and can be found connected to the proximal portion of the heavy chains. Multiple Clathrin molecules have the ability to form a variety of complex shapes when they interact, they can form 5 or 6 sided rings with the 5 sided kind having a greature curvature and when enough get together they can form ...
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article{1864472, abstract = {Endocytosis is a crucial mechanism by which eukaryotic cells internalize extracellular and plasma membrane material, and it is required for a multitude of cellular and developmental processes in unicellular and multicellular organisms. In animals and yeast, the best characterized pathway for endocytosis depends on the function of the vesicle coat protein clathrin. Clathrin-mediated endocytosis has recently been demonstrated also in plant cells, but its physiological and developmental roles remain unclear. Here, we assessed the roles of the clathrin-mediated mechanism of endocytosis in plants by genetic means. We interfered with clathrin heavy chain (CHC) function through mutants and dominant-negative approaches in Arabidopsis thaliana and established tools to manipulate clathrin function in a cell type-specific manner. The chc2 single mutants and dominant-negative CHC1 (HUB) transgenic lines were defective in bulk endocytosis as well as in internalization of ...
ALK a tyrosine kinase of the ALK family. Plays an important role in the development of the brain and exerts its effects on specific neurons in the nervous system. Translocated and expressed as a fusion protein in anaplastic lymphoma. About one third of large-cell lymphomas are caused by a t(2;5)(p23;q35) translocation that fuses ALK to nucleophosmin (NPM1A). Other cases caused by fusions of ALK to moesin, non-muscle myosin heavy chain 9, clathrin heavy chain and other genes. Several fusions also seen in inflammatory myofibroblastic tumors, and expression has been briefly noted in a range of tumors Note: This description may include information from UniProtKB ...
Immunogen = synthetic peptide: E E D P A A A F L A Q Q E S E I A G I E N D, corresp. to amino acids 23-44 of Cow Clathrin light chain. ...
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Eps15 is a substrate of the EGF receptor, and exhibits homology with the yeast protein End3, a protein involved in the endocytosis of the α factor in S. cerevisiae (Fazioli et al., 1993; Benedetti et al., 1994). Recently, Eps15 has been shown to bind directly to the ear of α-adaptin, a component of the AP-2 complex (Benmerah et al., 1995). In this paper, we have investigated the possible role of Eps15 in EGF receptor endocytosis. We have shown that Eps15 phosphorylation is mediated by the EGF receptor, and not by PDGF or insulin receptors, which suggest a possible function of Eps15 specifically in the endocytosis of EGF receptors. Immunoprecipitation studies revealed that Eps15 can be co-immunoprecipitated with the EGF receptor. Moreover, the association of Eps15 with the EGF receptor increased dramatically after activation of the receptor, while the association of Eps15 with AP-2 or clathrin LC appeared to occur independently of EGF. The association of Eps15 to the EGF receptor has not been ...
SSO mediated functional uptake in MHT cells is AP2M1 dependent and clathrin independent. (A) MHT cells were treated with 25 nM control, AP2M1, clathrin or RNA
SMAP2 immunoprecipitated clathrin and AP-1 through a putative clathrin-binding domain and a CALM-binding domain, and SMAP2 mutants that did not interact with clathrin or AP-1 could not localize to recycling ...
Plasmid pSNAP-CLC-SNAP from Dr. Xiaowei Zhuangs lab contains the insert Clathrin, light polypeptide (LCa) and is published in Nat Methods. 2011 Jun;8(6):499-508. Epub 2011 May 8. This plasmid is available through Addgene.
Plasmid mEos4a-Clathrin-15 from Dr. Michael Davidsons lab contains the insert Clathrin. This plasmid is available through Addgene.
The present invention relates in a first aspect to a method of coating surfaces of substrates with a lattice-like structure. In particular, the present invention relates to an in vitro method of coating surfaces by binding of epsin or a fragment thereof on the surface and, thereafter, binding of a compound forming the lattice like structure, in particular, binding of the clathrin heavy chain, to the epsin bound on the surface, thus, obtaining a coated substrate having a lattice like structure on the surface. In another aspect, the present invention relates to an in vitro method of producing nanometer-sized liposomes having a clathrin structure on its surface. In addition, substrates, like elements or devices, with coated surfaces having a lattice-like structure on the surface are provided obtainable by a method according to the present invention.
VOLUME 21 ISSUE 12 12 2011 1655 1661 Novel functions of endocytic player clathrin in mitosis Wenxiang Fu Qing Jiang and Chuanmao Zhang The MOE Key Laboratory of Cell Proliferation and Differentiation and the State Key Laboratory of Bio membrane and Membrane Biotechnology College of Life Sciences Peking University Beijing 100871 China Correspondence Chuanmao Zhang Tel 86 10 62757173 E mail zhangcm pku edu cn Clathrin has been widely recognized as a pivotal player in endocytosis in which several adaptors and accessory proteins are involved Recent studies suggested that clathrin is also essential for cell division Here this review mainly focuses on the clathrin dependent mechanisms involved in spindle assembly and chromosome alignment In mitosis clathrin forms a complex with phosphorylated TACC3 to ensure spindle stability and proper chromosome alignment The clathrin regulated mechanism in mitosis requires the crosstalk among clathrin spindle assembly factors SAFs Ran GTP and mitotic kinases ...
mmmmm cow brains the concept centers on a particular protein called clathrin which has a unique knack for assembling itself into versatile structures that foster the formation of complex molecules clathrin is present in every cell in the human body but cows possess a vast wealth of it in their bovine brains that make them an ideal source for the stuff and given the right biochemical directions researchers think they can coax clathrin into creating better batteries and solar cells http www popsci com science article - protein-cow-brains-could-build-better-batteries-solar-cells
/ X YOUTH Schwartz & et SOCIETY al. / IDENTITY / DECEMBER AND AGENCY 2005 IDENTITY AND AGENCY IN EMERGING ADULTHOOD: Two Developmental Routes in the Individualization Process SETH
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Doskonała propozycja dla Pań, które chcą szybko odświeżyć fryzurę! Suchy szampon do włosów Indola Style Reviver zapewnia naturalną objętość i matowy efekt.
Po wypadku grupa znajomych trafia do opustoszałego szpitala. Psychopatyczne zachowanie personelu sprawia, że pacjenci chcą jak najszybciej stamtąd uciec. ...
Pets are a treasured part of the family, but theyre also a smelly part of the family. Whether youre tackling little box smells, dog accidents, or the general scent of
Endocytosis is an essential phenomenon in eukaryotic cells. In animal cells, dynamin and clathrin play central roles in vesicle formation in the process of endocytosis, but the roles of similar proteins in plants are less well understood. Here, we observed the localization pattern and behavior of GFP-labeled ,i,Arabidopsis,/i, dynamin-related proteins (DRP1A and DRP2B), and clathrin light chain (AtCLC) around the plasma membrane in tobacco suspension cells by using variable incidence angle fluorescence microscopy (VIAFM). GFP fusions of DRP1A, DRP2B and AtCLC were observed as dot-like puncta 200-500 nm in diameter. The puncta moved to and away from the cell surface or also assembled and disassembled. The localization pattern and behavior of the puncta were similar to those of animal dynamin and clathrin signals reported previously. These results raise the possibility that DRP1A, DRP2B and AtCLC are involved in membrane trafficking around the plasma membrane, including endocytosis.. ...
Researchers of the group of cellular and molecular neurobiology of the Bellvitge Biomedical Research Institute and the University of Barcelona, led by researcher Artur Llobet, have shown that synaptic levels of the protein clathrin are a determinant factor for synaptic plasticity of neurons.
Thermodynamics of protein-mediated membrane deformation â application to clathrin dependent and clathrin independent endocytosis (2009 ...
Rabbit Polyclonal Anti-Clathrin interactor 1 Antibody. Validated: WB, ICC/IF, IHC, IHC-P. Tested Reactivity: Human, Mouse, Rat. 100% Guaranteed.
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DI-fusion, le Dépôt institutionnel numérique de lULB, est loutil de référencementde la production scientifique de lULB.Linterface de recherche DI-fusion permet de consulter les publications des chercheurs de lULB et les thèses qui y ont été défendues.
CHC of New London started in the summer of 1992 in partnership with Lawrence and Memorial Hospital and the city, taking over a city-run clinic that had been in existence since 1970. The partnership then won state and federal support in subsequent months ...
EpsinR is a clathrin-coated vesicle (CCV) enriched 70-kD protein that binds to phosphatidylinositol-4-phosphate, clathrin, and the gamma appendage domain of the adaptor protein complex 1 (AP1). In cells, its distribution overlaps with the perinuclear pool of clathrin and AP1 adaptors. Overexpression disrupts the CCV-dependent trafficking of cathepsin D from the trans-Golgi network to lysosomes and the incorporation of mannose-6-phosphate receptors into CCVs. These biochemical and cell biological data point to a role for epsinR in AP1/clathrin budding events in the cell, just as epsin1 is involved in the budding of AP2 CCVs. Furthermore, we show that two gamma appendage domains can simultaneously bind to epsinR with affinities of 0.7 and 45 microM, respectively. Thus, potentially, two AP1 complexes can bind to one epsinR. This high affinity binding allowed us to identify a consensus binding motif of the form DFxDF, which we also find in gamma-synergin and use to predict that an uncharacterized EF-hand
Assembly protein recruiting clathrin and adapter protein complex 2 (AP2) to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly. May be required to determine the amount of membrane to be recycled, possibly by regulating the size of the clathrin cage. Involved in AP2-dependent clathrin-mediated endocytosis at the neuromuscular junction. Plays a crucial role in fetal and adult hematopoiesis, and normal prenatal and postnatal growth and viability.
The nuclear export signal within clathrin assembly lymphoid myeloid leukemia protein (CALM) is critical for in vitro immortalization of cells by CALM-AF10. (a)
Clathrin (see MIM 118955)-mediated endocytosis is a major mechanism for internalization of proteins and lipids. Members of the connecdenn family, such as DENND1A, function as guanine nucleotide exchange factors (GEFs) for the early endosomal small GTPase RAB35 (MIM 604199) and bind to clathrin and clathrin adaptor protein-2 (AP2; see MIM 601024). Thus, connecdenns link RAB35 activation with the clathrin machinery (Marat and McPherson, 2010 [PubMed 20154091]).[supplied by OMIM, Nov 2010 ...
Katya Heldwein, PhD, Principal Investigator. Katya received her PhD from Oregon Health Sciences University in Portland, OR where she studied ligand recognition by bacterial transcription regulators using x-ray crystallography in the laboratory of Richard Brennan. She then did her postdoctoral work at Harvard Medical School in the laboratory of Stephen Harrison where she initially worked on clathrin adaptor complexes and later delved into herpesvirus cell entry. She opened her own laboratory at Tufts University School of Medicine in the Fall of 2006.. ...
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Reactome is pathway database which provides intuitive bioinformatics tools for the visualisation, interpretation and analysis of pathway knowledge.
Control of E-cadherin apical localisation and morphogenesis by a SOAP-1/AP-1/clathrin pathway in C. elegans epidermal cells. ...
Mills IG, Praefcke GJ, Vallis Y, Peter BJ, Olesen LE, Gallop JL, Butler PJ, Evans PR, McMahon HT. EpsinR: an AP1/clathrin interacting protein involved in vesicle trafficking. J Cell Biol. 2003 Jan 20;160(2):213-22. Epub 2003 Jan 21. PMID:12538641 doi:http://dx.doi.org/10.1083/jcb.200208023 ...
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In the present work, we have investigated mechanisms involved in the nucleotide-dependent regulation of clathrin-coated pit nucleation at the synapse. Our results implicate ARF6 in this process and demonstrate two effects of the GTP-bound form of this small GTPase; stimulation of the recruitment of clathrin/AP-2 to presynaptic membranes and binding plus activation of PIPKIγ. They also suggest that the two effects are related and that PI(4,5)P2 production by PIPKIγ stimulation represents the major mechanism through which ARF6 enhances clathrin/AP-2 recruitment. The action of GTP-ARF6 on clathrin/AP-2 recruitment mimics the effect of GTPγs, and its effects are antagonized by experimental manipulations that prevent either ARF activation (i.e., dominant-negative ARF6) or PI(4,5)P2 production and availability (i.e., kinase inhibition, PIPKIγ depletion, and PI(4,5)P2 hydrolysis by synaptojanins inositol 5′-phosphatase domain). These results strongly indicate that enhanced clathrin coat ...
Zika virus (ZIKV) infections can cause microcephaly and neurological disorders. However, the early infection events of ZIKV in neural cells remain to be characterized. Here, by using a combination of pharmacological and molecular approaches and the human glioblastoma cell T98G as a model, we first observed that ZIKV infection was inhibited by chloroquine and NH4Cl, indicating a requirement of low intracellular pH. We further showed that dynamin is required as the ZIKV entry was affected by the specific inhibitor dynasore, small interfering RNA (siRNA) knockdown of dynamin, or by expressing the dominant-negative K44A mutant. Moreover, the ZIKV entry was significantly inhibited by chlorpromazine, pitstop2, or siRNA knockdown of clathrin heavy chain, indicating an involvement of clathrin-mediated endocytosis. In addition, genistein treatment, siRNA knockdown of caveolin-1, or overexpression of a dominant-negative caveolin mutant impacted the ZIKV entry, with ZIKV particles being observed to colocalize with
In the present study, we demonstrated that clathrin and AP-1 are required for the retrograde transport from recycling endosomes to the Golgi. CTxB appeared to reach recycling endosomes in the clathrin- or AP-1-knockdown cells, similar to in control cells, suggesting that clathrin and AP-1 are not essential for the transport of CTxB from the plasma membrane through early endosomes to recycling endosomes. It has been shown that clathrin localizes to the TGN, early endosomes and the plasma membrane (Brodsky, 2012). We showed that CHC also localized to recycling endosomes. CHC colocalized with the recycling endosome proteins, Rab11, Tfn and SMAP2 in COS-1 cells (in which the Golgi, early endosomes and recycling endosomes are spatially distinct) (Lee et al., 2015; Misaki et al., 2007; Uchida et al., 2011). The recycling endosomes that were dispersed from the perinuclear region to the cytoplasm by nocodazole treatment remained positive for CHC. The localization of AP-1 to recycling endosomes (Folsch ...
Link to Pubmed [PMID] - 20486136. Bioessays 2010 Jun;32(6):496-504. Clathrin and the endocytosis machinery has recently been described as being required in mammalian cells for the internalization of large particles including pathogenic bacteria, fungi, and large viruses. These apparently unexpected observations, within the framework of the classical mechanisms for the formation of clathrin-coated vesicles, are now considered as examples of a new non-classical function of clathrin, which can promote the internalization of membrane domains associated to planar clathrin lattices. The role of actin downstream of clathrin seems to be critical for this still poorly characterized process. The historical frontier between endocytosis and phagocytosis is vanishing in the light of this new role for clathrin.. http://www.ncbi.nlm.nih.gov/pubmed/20486136 ...
Good News. Last night the Third Floor of the Outer Ward was published over at & Magazine. Bryan Fazekas and Handley Jackson did the editing, Robin Irwin provided the cover, and Ron Redmond takes care letting people know its out there. ...
410 Medical, a company out of Durham, North Carolina, is releasing in the U.S. its LifeFlow Rapid Infuser for treating patients afflicted by sepsis or shoc
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PICALM, the gene encoding phosphatidylinositol-binding clathrin assembly (picalm) protein, was recently shown to be associated with risk of Alzheimer disease (AD). Picalm is a key component of clathrin-mediated endocytosis. It recruits clathrin and adaptor protein 2 (AP-2) to the plasma membrane and, along with, AP-2 recognizes target proteins. The attached clathrin triskelions cause membrane deformation around the target proteins enclosing them within clathrin-coated vesicles to be processed in lysosomes or endosomes. We examined the distribution of picalm in control and AD brain tissue and measured levels of picalm messenger RNA (mRNA) by real-time polymerase chain reaction. Immunolabeling of brain tissue showed that picalm is predominately present in endothelial cells. This was further supported by the demonstration of picalm in human cerebral microvascular cells grown in culture. Picalm mRNA was elevated in relation to glyceraldehyde-3-phosphate dehydrogenase but not factor VIII-related ...
Backues, S.K. and Bednarek, S.Y. (2010). Arabidopsis Dynamin-Related Protein 1A polymers bind, but do not tubulate, liposomes. Biochem. Biophys. Res. Commun. 393, 734-739 [PDF]. Konopka, C. A. and Bednarek, S. Y. (2008). Comparison of the Dynamics and Functional Redundancy of the Arabidopsis Dynamin-Related Isoforms DRP1A and DRP1C during Plant Development. Plant Physiol. 147, 1590-1602. [PDF]. Konopka, C. A., Backues, S. K. and Bednarek, S. Y. (2008). Dynamics of Arabidopsis Dynamin-Related Protein 1C and a Clathrin Light Chain at the Plasma Membrane. Plant Cell 20, 1363-1380. [PDF]. Park, S., Rancour, D.M., and Bednarek, S.Y. (2008). In Planta analysis of the cell cycle-dependent localization of AtCDC48A and its critical roles in cell division, expansion and differentiation. Plant Phys. 148, 246-258 [PDF]. Park, S., Rancour, D.M., and Bednarek, S.Y. (2007). Protein domain-domain interactions and requirements for the negative regulation of Arabidopsis CDC48/P97 by the Plant Ubiquitin Regulatory ...
During clathrin-mediated endocytosis, it has been thought that the sensing and binding of the clathrin adaptor protein AP2 to cargo and lipids leads to the recruitment of clathrin, nucleating the formation of a clathrin-coated pit. Henne et al. have now found that this process of AP2 binding may not in fact represent either the first or the nucleation event of endocytosis. Instead, ubiquitous proteins called FCHo1/2 (F-BAR proteins) bind to the plasma membrane and define the sites of endocytosis independently of AP2. The F-BAR protein can generate very low curvatures and, at higher concentrations, generates higher curvatures like those required at the neck of budding vesicles. The C terminus of the protein has a μ-homology domain (with homology to the μ domain of the AP2 complex) that interacts with Eps15 and intersectin and via these proteins recruits AP2, which further recruits clathrin. Thus, a curvature-inducing protein can act to nucleate clathrin-coated pit assembly during ...
Steps in CCV assembly and links to structures and information around clathrin-coated vesicle formation and other forms of vesicle budding
Glyvuk et al (2010) argue that the CME of SV membranes represents a kinetic bottleneck of the recycling pathway. Under conditions of sustained activity BE provides a compensatory mechanism to balance high exocytic load with matching endocytic activity. Vacuolar membrane invaginations are then consumed by undefined budding events that chop these membranes into small vesicles that may re‐enter the SV cycle (Figure 1A). It is this consumption step that the authors envision to depend on AP‐1/σ1B (Figure 1B). The experimental evidence for this model at present remains indirect. AP‐1, as its relative AP‐2, is one of the major recruitment factors for clathrin and loss of either protein complex results in depletion of clathrin‐coated pits from TGN/endosomes or the plasmalemma, respectively. Why then do AP‐1/σ1B‐KO mice accumulate clathrin‐coated pits on endosome‐like vacuoles? One possibility is that other σ1 isoproteins such as σ1A do a poor job in functionally replacing σ1B on ...
Established in 2000, the Dental Center of Stamford was founded by area citizens and became part of CHC, Inc. in 2005. It is the hub for a network of CHC dental services throughout Stamford. When comprehensive medical services were added in 2009, the Center became known as the Franklin Street Community Health Center ...
In the second lecture, the next steps in viral infection are described. Endocytosis of plasma membrane bound viruses can occur via a number of mechanisms including caveolar, clathrin, non-clathrin, or lipid raft mediated pathways. The internalized vi
The vesicle simulation is available in two forms, one having enough for about one and a half vesicles (vesicle.obj) and the other having enough for about three (vesicle2.obj). Both can use either the vesicle_hub.tmpl or the vesicle_no_hub.tmpl template files (the first contains a sphere at the centre of each clathrin and is more polished visually, the second is faster). Note that in some runs of the simulation many fragments of vesicles form, rather than the few complete structures ...
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Chromosome 1; Chromosome 2; Chromosome 11; Chromosome 17; Chromosome 19; Translocation : t(1;2)(q25;p23); Translocation : t(2;2)(p23;q13); Translocation : t(2;11)(p23;p15); Translocation : t(2;17)(p23;q23); Translocation : t(2;19)(p23;p13); atypical fibromyxoid tumor (alias); pseudosarcomatous fibromyxoid tumor (alias); plasma cell granuloma (alias); pseudosarcomatous myofibrotic proliferation (alias); postoperative spindle cell nodules (alias); inflammatory pseudotumor (alias); Solid Tumors Section; Clathrin Heavy Chains; TPM3 protein, human; TPM4 protein, human; anaplastic lymphoma kinase; cysteinyl-tRNA synthetase; ran-binding protein ...
The lipid mediator sphingosine 1-phosphate (S1P) regulates a wide range of cellular activities, including vascular maturation, angiogenesis, and immune-cell trafficking. Among the five known receptors for S1P (S1PR1-S1PR5), S1PR1 is a critical regulator of lymphocyte trafficking: its signaling is required for lymphocyte egress from lymphoid organs, while its down-modulation by agonist-induced internalization is a prerequisite for lymphocyte entry into lymphoid organs from the bloodstream. Despite the importance of S1PR1 down-regulation in determining lymphocyte behavior, the molecular mechanism of its internalization in lymphocytes has not been defined. Here we show that agonist-induced S1PR1 internalization in T cells occurs via clathrin-mediated endocytosis and is regulated by moesin, an ezrin-radixin-moesin (ERM) family member. In S1P-stimulated T cells, S1PR1 relocalized within clathrin-coated vesicles (CCVs) and early endosomes, and S1PR1 internalization was blocked when clathrin was
It is known for decades, and most recently seen in dynamin knockout mice, that endocytosis continues when classical mechanisms are blocked or deleted. With the help of ubiquitin, yeast live without clathrin and fungi reveal still other alternatives in the absence of clathrin. We discovered a few years ago that 50 percent of the cell surface of many cells can be removed in seconds by Ca-dependent endocytosis that requires no classical endocytic player. This response is unrelated to either apoptosis or autophagy; cell cultures survive and even flourish in the wake of this remodeling. This form of endocytosis, relying on no known adapter or cytoskeleton, can quantitatively remove PD-1 receptors from the T-cell surface membrane, receptors whose inactivation is a key to activating immune responses. Thus, domain-dependent endocytosis can be concentrative as well as contributing to overall fluid-phase endocytosis. As for exocytosis, Ca stress-dependent exocytosis can rapidly increase membrane area by ...
Some identifications are effected where portions of the ridge detail in one impression are missing from the other. If latent to latent individualizations have linked multiple latent prints in a case and exemplars are later received, it is at the discretion of the agency whether to compare all of the latent impressions to the received exemplars. It is recommended to individually compare each of those associated latent prints to the received exemplars. It is acceptable to report latent to latent individualizations to an exemplar when only one of the latent impressions has been identified to the exemplar (Figure 1). Agency policy should address latent to latent comparisons ...
Mouse monoclonal MARG2a-1 Anti-Rat IgG2a heavy chain (FITC) (ab11671) has been cited in 1 publications. Find out more about the references
PhD Project - High resolution cryo-electron microscopy of clathrin cage networks at University of Warwick, listed on FindAPhD.com
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In this work, we have shown that RME‐8 and SNX‐1 are required to rescue MIG‐14 from degradation after its endocytosis. Our results showing the aberrant sorting and degradation of MIG‐14 in snx‐1 and rme‐8 mutants are quite similar to those earlier shown for CI‐M6PR after co‐depletion of Snx1 and Snx2, or single depletion of other retromer components, in mammalian cells (Rojas et al, 2007). Our results are also reminiscent of the aberrant sorting and degradation of the EGF‐R after siRNA‐mediated depletion of RME‐8 in mammalian cells (Girard and McPherson, 2008). In fact, this similarity in phenotype may indicate that a fraction of EGF‐Rs recycle through the retrograde endosome to Golgi pathway.. However, CI‐M6PR steady‐state levels were not reported to be reduced after siRNA‐mediated depletion of RME‐8 (Girard et al, 2005). Rather, CI‐M6PR was reported to aberrantly accumulate in or near the Golgi (Girard et al, 2005). We do not yet understand this apparent ...
Human IgG4 heavy chain小鼠单克隆抗体[5C7](ab1930)可与人样本反应并经ELISA实验严格验证,被1篇文献引用。所有产品均提供质保服务,中国75%以上现货。
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IJMS  | Free Full-Text | Characterization of a Gene Encoding Clathrin Heavy Chain in Maize Up-Regulated by Salicylic Acid,...IJMS | Free Full-Text | Characterization of a Gene Encoding Clathrin Heavy Chain in Maize Up-Regulated by Salicylic Acid,...

... a three-legged triskelion composed of three clathrin heavy chains (CHCs) and three light chains (CLCs), plays a critical role ... In this study, the genes ZmCHC1 and ZmCHC2 encoding clathrin heavy chain in maize were cloned and characterized for the first ... in clathrin-mediated endocytosis (CME) in eukaryotic cells. ... An analysis of clathrin heavy chain and light chain sequences ... Clathrin, a three-legged triskelion composed of three clathrin heavy chains (CHCs) and three light chains (CLCs), plays a ...
more infohttp://www.mdpi.com/1422-0067/14/7/15179/htm

Picalm - Phosphatidylinositol-binding clathrin assembly protein - Mus musculus (Mouse) - Picalm gene & proteinPicalm - Phosphatidylinositol-binding clathrin assembly protein - Mus musculus (Mouse) - Picalm gene & protein

May be required to determine the amount of membrane to be recycled, possibly by regulating the size of the clathrin cage. ... Involved in AP2-dependent clathrin-mediated endocytosis at the neuromuscular junction. Plays a crucial role in fetal and adult ... to cell membranes at sites of coated-pit formation and clathrin-vesicle assembly. ... Assembly protein recruiting clathrin and adapter protein complex 2 (AP2) ...
more infohttp://www.uniprot.org/uniprot/Q7M6Y3

Clathrin is spindle-associated but not essential for mitosis. - Nuffield Department of Surgical SciencesClathrin is spindle-associated but not essential for mitosis. - Nuffield Department of Surgical Sciences

... was developed in which the endogenous clathrin heavy chain alleles were replaced with the human clathrin heavy chain under the ... and we used this to explore the significance of clathrin heavy chain expression for cell cycle progression. We confirmed using ... ploidy and the recovery kinetics following cell cycle arrest with nocodazole were unchanged by repressing clathrin heavy chain ... We show an effect on the G2/M phase population of clathrin knockdown in HEK293 cells but show that repressing clathrin ...
more infohttps://www.nds.ox.ac.uk/publications/817498

Clathrin, heavy chain (TD.1) | ALZFORUMClathrin, heavy chain (TD.1) | ALZFORUM

Immunogen = N-terminus of human Clathrin heavy chain. Specificity. Clathrin heavy chain ...
more infohttps://www.alzforum.org/antibodies/clathrin-heavy-chain-td1

Clathrin, heavy chain (H-300) | ALZFORUMClathrin, heavy chain (H-300) | ALZFORUM

If you know of any papers that use this antibody, please contact us at antibodies [at] alzforum [dot] org for consideration in the References section.. ...
more infohttps://www.alzforum.org/antibodies/clathrin-heavy-chain-h-300

Clathrin light and heavy chain interface: alpha-helix binding superhelix loops via critical tryptophans.  - PubMed - NCBIClathrin light and heavy chain interface: alpha-helix binding superhelix loops via critical tryptophans. - PubMed - NCBI

Clathrin light and heavy chain interface: alpha-helix binding superhelix loops via critical tryptophans.. Chen CY1, Reese ML, ... LC binding to clathrin heavy chain (HC) was characterized by genetic and structural approaches. The core interactions were ... 2. Parallel interaction at the C-termini of clathrin heavy and light chains. Plate growth and β-galactosidase (β-gal) filter ... Clathrin light and heavy chain interface: α-helix binding superhelix loops via critical tryptophans ...
more infohttps://www.ncbi.nlm.nih.gov/pubmed/12426379

clathrin, Heavy Chain (Hc) (CLTC) Antibodiesclathrin, Heavy Chain (Hc) (CLTC) Antibodies

clathrin heavy chain , Clathrin Heavy Chain family member (chc-1) , clathrin heavy chain 1 , clathrin heavy-chain , clathrin, ... clathrin, heavy chain (Hc) , clathrin, heavy polypeptide a , clathrin, heavy polypeptide a (Hc) , clathrin, heavy chain (Hc) L ... Top referenced anti-clathrin, Heavy Chain (Hc) Antibodies. Show all anti-clathrin, Heavy Chain (Hc) (CLTC) Antibodies with ... More product categories related to clathrin, Heavy Chain (Hc) Antibody * 166 anti-clathrin, Heavy Chain (Hc) Primary Antibodies ...
more infohttps://www.antibodies-online.com/abstract/clathrin%2C+Heavy+Chain+

Clathrin Heavy Chain 2/CHC22/CLTCL1 Research Products: Novus BiologicalsClathrin Heavy Chain 2/CHC22/CLTCL1 Research Products: Novus Biologicals

Browse our Clathrin Heavy Chain 2/CHC22/CLTCL1 product catalog backed by our Guarantee+. ... Clathrin Heavy Chain 2/CHC22/CLTCL1 products available through Novus Biologicals. ... Diseases related to Clathrin Heavy Chain 2/CHC22/CLTCL1. Discover more about diseases related to Clathrin Heavy Chain 2/CHC22/ ... Bioinformatics Tool for Clathrin Heavy Chain 2/CHC22/CLTCL1. Discover related pathways, diseases and genes to Clathrin Heavy ...
more infohttps://www.novusbio.com/common-name/clathrin-heavy-chain-2-chc22-cltcl1

Clathrin Heavy Chain 1/CHC17 Antibody (NBP2-49293): Novus BiologicalsClathrin Heavy Chain 1/CHC17 Antibody (NBP2-49293): Novus Biologicals

Rabbit Polyclonal Anti-Clathrin Heavy Chain 1/CHC17 Antibody. Validated: WB, ICC/IF, IHC, IHC-P. Tested Reactivity: Human, ... Home » Clathrin Heavy Chain 1/CHC17 » Clathrin Heavy Chain 1/CHC17 Antibodies » Clathrin Heavy Chain 1/CHC17 Antibody ... Blogs on Clathrin Heavy Chain 1/CHC17. There are no specific blogs for Clathrin Heavy Chain 1/CHC17, but you can read our ... PTMs for Clathrin Heavy Chain 1/CHC17 Antibody (NBP2-49293). Learn more about PTMs related to Clathrin Heavy Chain 1/CHC17 ...
more infohttps://www.novusbio.com/products/clathrin-heavy-chain-1-chc17-antibody_nbp2-49293

Clathrin heavy chain plays multiple roles in polarizing the Drosophila oocyte downstream of Bic-D | DevelopmentClathrin heavy chain plays multiple roles in polarizing the Drosophila oocyte downstream of Bic-D | Development

Clathrin heavy chain (Chc) co-immunopurifies with Bic-D in embryos and ovaries, and a fraction of Chc colocalizes with Bic-D. ... Clathrin heavy chain plays multiple roles in polarizing the Drosophila oocyte downstream of Bic-D ... Clathrin heavy chain plays multiple roles in polarizing the Drosophila oocyte downstream of Bic-D ... Clathrin heavy chain plays multiple roles in polarizing the Drosophila oocyte downstream of Bic-D ...
more infohttp://dev.biologists.org/content/early/2014/04/09/dev.099432

Clathrin heavy chain is required for pinocytosis, the presence of large vacuoles, and development in Dictyostelium. | JCBClathrin heavy chain is required for pinocytosis, the presence of large vacuoles, and development in Dictyostelium. | JCB

Similarly, Northern blots showed an absence of clathrin heavy chain mRNA. Clathrin heavy chain-deficient Dictyostelium cells ... with an anti-clathrin heavy chain antiserum revealed that mutant cells contained undetectable amounts of clathrin heavy chain ... Clathrin heavy chain is required for pinocytosis, the presence of large vacuoles, and development in Dictyostelium.. T J ... Clathrin heavy chain is required for pinocytosis, the presence of large vacuoles, and development in Dictyostelium. ...
more infohttp://jcb.rupress.org/content/118/6/1371?ijkey=78b8dafb45fac394758e98caa0558201de029fdb&keytype2=tf_ipsecsha

2610002d18rik, clathrin heavy chain linker domain containing 1 - Creative Biogene2610002d18rik, clathrin heavy chain linker domain containing 1 - Creative Biogene

Creative Biogene offers challenging job opportunities for people looking for career growth in an entrepreneurial environment that recognizes individual contributions. More ...
more infohttps://www.creative-biogene.com/symbolsearch_2610002d18rik.html

Transformation by Rous sarcoma virus induces clathrin heavy chain phosphorylation. | Journal of Cell Biology | Rockefeller...Transformation by Rous sarcoma virus induces clathrin heavy chain phosphorylation. | Journal of Cell Biology | Rockefeller...

Clathrin heavy chain is a substrate for pp60v-src in vitro. Cleveland analysis of the in vivo and in vitro clathrin heavy chain ... Transformation by Rous sarcoma virus induces clathrin heavy chain phosphorylation. J Martin-Perez, J Martin-Perez ... The phosphorylation of clathrin heavy chain in transformed cells may be linked to previously observed transformation-dependent ... J Martin-Perez, D Bar-Zvi, D Branton, R L Erikson; Transformation by Rous sarcoma virus induces clathrin heavy chain ...
more infohttps://rupress.org/jcb/article/109/2/577/55663/Transformation-by-Rous-sarcoma-virus-induces

T Cell Receptor Engagement Leads to Phosphorylation of Clathrin Heavy Chain during Receptor Internalization  | Journal of...T Cell Receptor Engagement Leads to Phosphorylation of Clathrin Heavy Chain during Receptor Internalization | Journal of...

... clathrin and adaptor proteins (13). Clathrin is composed of three ∼192-kD heavy chains bound to three ∼25-kD light chains. ... Abbreviations used in this paper: BCR, B cell receptor; CCV, clathrin-coated vesicle; CHC, clathrin heavy chain; EGFR, ... in the region of the heavy chain that interacts with light chain and regulates assembly of the clathrin triskelion (38). Our ... T Cell Receptor Engagement Leads to Phosphorylation of Clathrin Heavy Chain during Receptor Internalization Victoria L. Crotzer ...
more infohttps://rupress.org/jem/article/199/7/981/40109/T-Cell-Receptor-Engagement-Leads-to

Anti Clathrin Heavy Chain Antibody (PrecisionAb™ Monoclonal Antibody) | Bio-RadAnti Clathrin Heavy Chain Antibody (PrecisionAb™ Monoclonal Antibody) | Bio-Rad

Clathrin heavy chain antibody for detecting human clathrin heavy chain. Validated on up to 12 cell lysates for western blotting ... Mouse anti Clathrin Heavy Chain. Mouse anti human clathrin heavy chain antibody recognizes clathrin heavy chain, also known as ... Mouse anti Human clathrin heavy chain antibody recognizes clathrin heavy chain , also known as CLTC, CHC, clathrin heavy chain ... Mouse anti human clathrin heavy chain antibody recognizes clathrin heavy chain, also known as clathrin heavy chain on ...
more infohttps://www.bio-rad-antibodies.com/monoclonal/human-clathrin-heavy-chain-antibody-vma00411.html

Gentaur Molecular :Exbio \ Clathrin heavy chain \ 11-526-C025Gentaur Molecular :Exbio \ Clathrin heavy chain \ 11-526-C025

Clathrin heavy chain \ 11-526-C025 for more molecular products just contact us ... WP884: Electron Transport Chain. Related Genes :. [CLTC CLH17 CLTCL2 KIAA0034] Clathrin heavy chain 1 (Clathrin heavy chain on ... Clathrin heavy chain 2 (Clathrin heavy chain on chromosome 22) (CLH-22). [Picalm Calm] Phosphatidylinositol-binding clathrin ... We have also other products like : Clathrin heavy chain. Related products : Clathrin heavy chain ...
more infohttp://www.antibody-antibodies.com/product_det.php?id=208556&supplier=search&name=Clathrin%20heavy%20chain

Sheep anti-human Clathrin Heavy Chain 2 (CHC22)-Angio-ProteomieSheep anti-human Clathrin Heavy Chain 2 (CHC22)-Angio-Proteomie

Sheep anti-human Clathrin Heavy Chain 2 (CHC22), High Quality-Price Ratio Products and Services. Quality Assurance Guaranteed. ... Sheep Polyclonal anti-human Clathrin Heavy Chain 2 (CHC22) Sheep Polyclonal anti-human Clathrin Heavy Chain 2 (CHC22). ... Detects human Clathrin Heavy Chain 2/CHC22 in direct ELISAs and Western blots. In direct ELISAs, less than1% cross-reactivity ... This antibody was produced from a sheep immunized with purified human clathrin heavy chain 2/chc22 protein. ...
more infohttp://www.angioproteomie.com/commerce/ccp3384-sheep-polyclonal-anti-human-clathrin-heavy-chain--hap-5101.htm

Picalm phosphatidylinositol binding clathrin assembly protein [Mus musculus (house mouse)] - Gene - NCBIPicalm phosphatidylinositol binding clathrin assembly protein [Mus musculus (house mouse)] - Gene - NCBI

clathrin binding ISO Inferred from Sequence Orthology. more info. clathrin heavy chain binding ISO Inferred from Sequence ... Cargo recognition for clathrin-mediated endocytosis, organism-specific biosystem (from REACTOME) Cargo recognition for clathrin ... Clathrin derived vesicle budding, organism-specific biosystem (from REACTOME) Clathrin derived vesicle budding, organism- ... Clathrin-mediated endocytosis, organism-specific biosystem (from REACTOME) Clathrin-mediated endocytosis, organism-specific ...
more infohttps://www.ncbi.nlm.nih.gov/gene/?term=233489

Clathrin - WikipediaClathrin - Wikipedia

The clathrin triskelion is composed of three clathrin heavy chains interacting at their C-termini, each ~190 kDa heavy chain ... The main clathrin heavy chain, located on chromosome 17 in humans, is found in all cells. A second clathrin heavy chain gene, ... The three heavy chains provide the structural backbone of the clathrin lattice, and the three light chains are thought to ... It forms a triskelion shape composed of three clathrin heavy chains and three light chains. When the triskelia interact they ...
more infohttps://en.wikipedia.org/wiki/Clathrin

Intersectin associates with synapsin and regulates its nanoscale localization and function | PNASIntersectin associates with synapsin and regulates its nanoscale localization and function | PNAS

CHC, clathrin heavy chain; Hsc70, heat shock cognate protein 70; ITSN1, intersectin 1. (C) Intersectin 1 and 2 colocalize with ... S4 I and J). Loss of intersectin 1/2 did not affect the nanoscale distribution of endophilin A1 or the clathrin adaptor AP2, ... 2010) Regulation of synaptic vesicle recycling by complex formation between intersectin 1 and the clathrin adaptor complex AP2 ... Fusing SVs are concomitantly replenished by compensatory endocytosis of SV membranes and clathrin-mediated reformation of SVs ( ...
more infohttp://www.pnas.org/content/114/45/12057.long

CATH Superfamily 1.25.40.10CATH Superfamily 1.25.40.10

FunFam 94149: Clathrin heavy chain. * Summary * Alignment * GO * EC * Taxonomy /* http://stackoverflow.com/questions/9141629/ ...
more infohttp://www.cathdb.info/version/v4_2_0/superfamily/1.25.40.10/funfam/94149/alignment

RCSB PDB - Protein Feature View 









 - Putative tyrosine-protein phosphatase auxilin - Q27974 (AUXI BOVIN)RCSB PDB - Protein Feature View - Putative tyrosine-protein phosphatase auxilin - Q27974 (AUXI BOVIN)

Recruits HSPA8/HSC70 to clathrin-coated vesicles and promotes uncoating of clathrin-coated vesicles (PubMed:15502813). Plays a ...
more infohttp://www.rcsb.org/pdb/protein/Q27974

Molecular characterization, developmental expression and immunolocalization of clathrin heavy chain in the ovary of the...Molecular characterization, developmental expression and immunolocalization of clathrin heavy chain in the ovary of the...

It is composed of three identical clathrin heavy chains (CHC), each with an attached light chain. We characterized the deduced ... 10]. Kokoza, V.A. & Raikhel, A.S. (1997). Ovarian- and somatic-specific transcripts of the mosquito clathrin heavy chain gene ... 11]. Kokoza, V.A., Snigirevskaya, E.S. & Raikhel, A.S. (1997). Mosquito clathrin heavy chain: analysis of protein structure and ... Molecular characterization, developmental expression and immunolocalization of clathrin heavy chain in the ovary of the ...
more infohttps://e-journal.sospublication.co.in/index.php/jalrb/article/view/149

Search: All Pfam signatures | InterPro | EMBL-EBISearch: All Pfam signatures | InterPro | EMBL-EBI

Clathrin, heavy chain/VPS, 7-fold repeat (IPR000547) Pfam signature: PF00637 Ran binding domain (IPR000156) Pfam signature: ... Clathrin, heavy chain, propeller repeat (IPR022365) Pfam signature: PF01394 Pheromone/general odorant binding protein ( ... Clathrin light chain (IPR000996) Pfam signature: PF01086 Galactose-1-phosphate uridyl transferase, N-terminal (IPR005849) Pfam ... Heat-labile enterotoxin, A chain (IPR001144) Pfam signature: PF01375 Heat-labile enterotoxin, B chain (IPR001835) Pfam ...
more infohttp://www.ebi.ac.uk/interpro/member-database/Pfam

Frontiers | SR-BI Mediated Transcytosis of HDL in Brain Microvascular Endothelial Cells Is Independent of Caveolin, Clathrin,...Frontiers | SR-BI Mediated Transcytosis of HDL in Brain Microvascular Endothelial Cells Is Independent of Caveolin, Clathrin,...

Using these approaches, we report that HDL internalization requires dynamin but not clathrin heavy chain and that its ... Using these approaches, we report that HDL internalization requires dynamin but not clathrin heavy chain and that its ... Depletion of clathrin heavy chain and SR-BI was accomplished by transfection of siRNA with HiPerfect transfection reagent ( ... For western blots, primary antibodies against the clathrin heavy chain (Santa Cruz: sc-6579), cav-1 (Santa Cruz: sc-894), PDZK1 ...
more infohttps://www.frontiersin.org/articles/10.3389/fphys.2017.00841/full
  • Consequently this work highlights the need for a more detailed molecular understanding of the recruitment and function of clathrin at the spindle, since the localisation but not the impact of clathrin on mitosis appears to be robust in plants, mammalian and chicken B-cells. (ox.ac.uk)
  • In other cell-lines silencing RNA has been used by others to knockdown clathrin expression resulting in an increase in the mitotic index of the cells. (ox.ac.uk)
  • We show an effect on the G2/M phase population of clathrin knockdown in HEK293 cells but show that repressing clathrin expression in the DKO-R cell-line has no effect on the size of this population. (ox.ac.uk)
  • Clathrin is spindle-associated but not essential for mitosis. (ox.ac.uk)
  • Here we test whether the recruitment of clathrin to the spindle is indicative of a critical functional contribution to mitosis. (ox.ac.uk)
  • However we find that the contribution of clathrin to mitosis is less robust and dependent on cellular context. (ox.ac.uk)
  • Additionally, we showed that the ploidy and the recovery kinetics following cell cycle arrest with nocodazole were unchanged by repressing clathrin heavy chain expression. (ox.ac.uk)
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