CLTC
Clathrin heavy chain 1 is a protein that in humans is encoded by the CLTC gene.[1][2]
Clathrin is a major protein component of the cytoplasmic face of intracellular organelles, called coated vesicles and coated pits. These specialized organelles are involved in the intracellular trafficking of receptors and endocytosis of a variety of macromolecules. The basic subunit of the clathrin coat is composed of three heavy chains and three light chains.[3]
Interactions
CLTC has been shown to interact with PICALM[4] and HGS.[5]
See also
References
- ^ Dodge GR, Kovalszky I, McBride OW, Yi HF, Chu ML, Saitta B, Stokes DG, Iozzo RV (Feb 1992). "Human clathrin heavy chain (CLTC): partial molecular cloning, expression, and mapping of the gene to human chromosome 17q11-qter". Genomics 11 (1): 174–8. doi:10.1016/0888-7543(91)90115-U. PMID 1765375.
- ^ Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S (Dec 1995). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1". DNA Res 1 (1): 27–35. doi:10.1093/dnares/1.1.27. PMID 7584026.
- ^ "Entrez Gene: CLTC clathrin, heavy chain (Hc)". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1213.
- ^ Tebar, F; Bohlander S K, Sorkin A (Aug. 1999). "Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic". Mol. Biol. Cell (UNITED STATES) 10 (8): 2687–702. ISSN 1059-1524. PMC 25500. PMID 10436022. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=25500.
- ^ Raiborg, C; Bache K G, Mehlum A, Stang E, Stenmark H (Sep. 2001). "Hrs recruits clathrin to early endosomes". EMBO J. (England) 20 (17): 5008–21. doi:10.1093/emboj/20.17.5008. ISSN 0261-4189. PMC 125612. PMID 11532964. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=125612.
Further reading
- Murphy JE, Keen JH (1992). "Recognition sites for clathrin-associated proteins AP-2 and AP-3 on clathrin triskelia.". J. Biol. Chem. 267 (15): 10850–5. PMID 1587861.
- Corvera S (1990). "Insulin stimulates the assembly of cytosolic clathrin onto adipocyte plasma membranes.". J. Biol. Chem. 265 (5): 2413–6. PMID 2154445.
- Scarmato P, Kirchhausen T (1990). "Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3.". J. Biol. Chem. 265 (7): 3661–8. PMID 2406259.
- Hanspal M, Luna E, Branton D (1984). "The association of clathrin fragments with coated vesicle membranes.". J. Biol. Chem. 259 (17): 11075–82. PMID 6147350.
- Nomura N, Miyajima N, Sazuka T, et al. (1995). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1 (supplement).". DNA Res. 1 (1): 47–56. doi:10.1093/dnares/1.1.47. PMID 7584028.
- Fausser JL, Ungewickell E, Ruch JV, Lesot H (1994). "Interaction of vinculin with the clathrin heavy chain.". J. Biochem. 114 (4): 498–503. PMID 8276759.
- Kedra D, Peyrard M, Fransson I, et al. (1997). "Characterization of a second human clathrin heavy chain polypeptide gene (CLH-22) from chromosome 22q11.". Hum. Mol. Genet. 5 (5): 625–31. doi:10.1093/hmg/5.5.625. PMID 8733129.
- Goodman OB, Krupnick JG, Gurevich VV, et al. (1997). "Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain.". J. Biol. Chem. 272 (23): 15017–22. doi:10.1074/jbc.272.23.15017. PMID 9169477.
- Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS (1997). "Identification and characterization of a nerve terminal-enriched amphiphysin isoform.". J. Biol. Chem. 272 (26): 16700–6. doi:10.1074/jbc.272.26.16700. PMID 9195986.
- McMahon HT, Wigge P, Smith C (1997). "Clathrin interacts specifically with amphiphysin and is displaced by dynamin.". FEBS Lett. 413 (2): 319–22. doi:10.1016/S0014-5793(97)00928-9. PMID 9280305.
- Foti M, Mangasarian A, Piguet V, et al. (1998). "Nef-mediated clathrin-coated pit formation.". J. Cell Biol. 139 (1): 37–47. doi:10.1083/jcb.139.1.37. PMC 2139808. PMID 9314527. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2139808.
- Dell'Angelica EC, Klumperman J, Stoorvogel W, Bonifacino JS (1998). "Association of the AP-3 adaptor complex with clathrin.". Science 280 (5362): 431–4. doi:10.1126/science.280.5362.431. PMID 9545220.
- Ramjaun AR, McPherson PS (1998). "Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites.". J. Neurochem. 70 (6): 2369–76. doi:10.1046/j.1471-4159.1998.70062369.x. PMID 9603201.
- ter Haar E, Musacchio A, Harrison SC, Kirchhausen T (1998). "Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker.". Cell 95 (4): 563–73. doi:10.1016/S0092-8674(00)81623-2. PMID 9827808.
- Laporte SA, Oakley RH, Zhang J, et al. (1999). "The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis.". Proc. Natl. Acad. Sci. U.S.A. 96 (7): 3712–7. doi:10.1073/pnas.96.7.3712. PMC 22359. PMID 10097102. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=22359.
- Turner CE, Brown MC, Perrotta JA, et al. (1999). "Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling.". J. Cell Biol. 145 (4): 851–63. doi:10.1083/jcb.145.4.851. PMC 2133183. PMID 10330411. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2133183.
- Hussain NK, Yamabhai M, Ramjaun AR, et al. (1999). "Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells.". J. Biol. Chem. 274 (22): 15671–7. doi:10.1074/jbc.274.22.15671. PMID 10336464.
- Ybe JA, Brodsky FM, Hofmann K, et al. (1999). "Clathrin self-assembly is mediated by a tandemly repeated superhelix.". Nature 399 (6734): 371–5. doi:10.1038/20708. PMID 10360576.
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PDB gallery
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1b89: CLATHRIN HEAVY CHAIN PROXIMAL LEG SEGMENT (BOVINE)
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1bpo: CLATHRIN HEAVY-CHAIN TERMINAL DOMAIN AND LINKER
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1c9i: PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN
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1c9l: PEPTIDE-IN-GROOVE INTERACTIONS LINK TARGET PROTEINS TO THE B-PROPELLER OF CLATHRIN
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1utc: CLATHRIN TERMINAL DOMAIN COMPLEXED WITH TLPWDLWTT
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This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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| Synaptic vesicle |
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SNAP25 · SNAP29
Syntaxin (STX1A, STX1B, STX2, STX3, STX4, STX5, STX6, STX7, STX8, STX10, STX11, STX12, STX16, STX17, STX18, STX19)
Munc-18: STXBP1 · STXBP2 · STXBP3 · STXBP4 · STXBP5 · STXBP6
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Other
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| COPI |
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| COPII |
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| RME/Clathrin |
CLTA · CLTB · CLTC
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| Caveolae |
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| Other/ungrouped |
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see also vesicular transport protein disorders
B memb: cead, trns (1A, 1C, 1F, 2A, 3A1, 3A2-3, 3D), othr
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