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]
References
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)”.
- ↑ 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. doi:10.1091/mbc.10.8.2687. ISSN 1059-1524. PMC 25500. PMID 10436022.
- ↑ 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.
Further reading
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.
- Dell’Angelica EC, Klumperman J, Stoorvogel W, Bonifacino JS (1998). “Association of the AP-3 adaptor complex with clathrin”. Science. 280 (5362): 431–4. Bibcode:1998Sci…280..431D. 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. Bibcode:1999PNAS…96.3712L. doi:10.1073/pnas.96.7.3712. PMC 22359. PMID 10097102.
- 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.
- 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. Bibcode:1999Natur.399..371Y. doi:10.1038/20708. PMID 10360576.
External links
External links
- Human CLTC genome location and CLTC gene details page in the UCSC Genome Browser.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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