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CLTC

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{For-multi|the Chinese vehicle testing standard|China Light-Duty Vehicle Test Cycle|the religious organization in Papua New Guinea|Christian Leaders' Training College}}

{{Infobox_gene}}

Clathrin heavy chain 1 is a protein that in humans is encoded by the CLTC gene.{{cite journal | vauthors = Dodge GR, Kovalszky I, McBride OW, Yi HF, Chu ML, Saitta B, Stokes DG, Iozzo RV | title = Human clathrin heavy chain (CLTC): partial molecular cloning, expression, and mapping of the gene to human chromosome 17q11-qter | journal = Genomics | volume = 11 | issue = 1 | pages = 174–8 |date=Feb 1992 | pmid = 1765375 | doi =10.1016/0888-7543(91)90115-U }}{{cite journal | vauthors = Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S | title = 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 | journal = DNA Res | volume = 1 | issue = 1 | pages = 27–35 |date=Dec 1995 | pmid = 7584026 | doi =10.1093/dnares/1.1.27 | doi-access = free }}

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.{{cite web | title = Entrez Gene: CLTC clathrin, heavy chain (Hc)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1213}}

Interactions

CLTC has been shown to interact with PICALM{{cite journal |last=Tebar |first=F |author2=Bohlander S K|author3=Sorkin A |date=Aug 1999 |title=Clathrin assembly lymphoid myeloid leukemia (CALM) protein: localization in endocytic-coated pits, interactions with clathrin, and the impact of overexpression on clathrin-mediated traffic |journal=Mol. Biol. Cell |volume=10 |issue=8 |pages=2687–702 | issn = 1059-1524| pmid = 10436022 |pmc=25500 | doi=10.1091/mbc.10.8.2687}} and HGS.{{cite journal |last=Raiborg |first=C |author2=Bache K G|author3=Mehlum A|author4=Stang E|author5=Stenmark H |date=Sep 2001 |title=Hrs recruits clathrin to early endosomes |journal=EMBO J. |volume=20 |issue=17 |pages=5008–21 | issn = 0261-4189| pmid = 11532964 |doi = 10.1093/emboj/20.17.5008 |pmc=125612 }}

See also

References

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Further reading

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  • {{cite journal | vauthors=Murphy JE, Keen JH |title=Recognition sites for clathrin-associated proteins AP-2 and AP-3 on clathrin triskelia. |journal=J. Biol. Chem. |volume=267 |issue= 15 |pages= 10850–5 |year= 1992 |doi=10.1016/S0021-9258(19)50096-5 |pmid= 1587861 |doi-access=free }}
  • {{cite journal | author=Corvera S |title=Insulin stimulates the assembly of cytosolic clathrin onto adipocyte plasma membranes. |journal=J. Biol. Chem. |volume=265 |issue= 5 |pages= 2413–6 |year= 1990 |doi=10.1016/S0021-9258(19)39811-4 |pmid= 2154445 |doi-access=free }}
  • {{cite journal | vauthors=Scarmato P, Kirchhausen T |title=Analysis of clathrin light chain-heavy chain interactions using truncated mutants of rat liver light chain LCB3. |journal=J. Biol. Chem. |volume=265 |issue= 7 |pages= 3661–8 |year= 1990 |doi=10.1016/S0021-9258(19)39644-9 |pmid= 2406259 |doi-access=free }}
  • {{cite journal |author3-link=Daniel Branton | vauthors=Hanspal M, Luna E, Branton D |title=The association of clathrin fragments with coated vesicle membranes. |journal=J. Biol. Chem. |volume=259 |issue= 17 |pages= 11075–82 |year= 1984 |doi=10.1016/S0021-9258(18)90624-1 |pmid= 6147350 |doi-access=free }}
  • {{cite journal | vauthors=Nomura N, Miyajima N, Sazuka T |title=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). |journal=DNA Res. |volume=1 |issue= 1 |pages= 47–56 |year= 1995 |pmid= 7584028 |doi=10.1093/dnares/1.1.47 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Fausser JL, Ungewickell E, Ruch JV, Lesot H |title=Interaction of vinculin with the clathrin heavy chain. |journal=J. Biochem. |volume=114 |issue= 4 |pages= 498–503 |year= 1994 |pmid= 8276759 |doi= 10.1093/oxfordjournals.jbchem.a124206}}
  • {{cite journal | vauthors=Kedra D, Peyrard M, Fransson I |title=Characterization of a second human clathrin heavy chain polypeptide gene (CLH-22) from chromosome 22q11. |journal=Hum. Mol. Genet. |volume=5 |issue= 5 |pages= 625–31 |year= 1997 |pmid= 8733129 |doi=10.1093/hmg/5.5.625 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Goodman OB, Krupnick JG, Gurevich VV |title=Arrestin/clathrin interaction. Localization of the arrestin binding locus to the clathrin terminal domain. |journal=J. Biol. Chem. |volume=272 |issue= 23 |pages= 15017–22 |year= 1997 |pmid= 9169477 |doi=10.1074/jbc.272.23.15017 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Ramjaun AR, Micheva KD, Bouchelet I, McPherson PS |title=Identification and characterization of a nerve terminal-enriched amphiphysin isoform. |journal=J. Biol. Chem. |volume=272 |issue= 26 |pages= 16700–6 |year= 1997 |pmid= 9195986 |doi=10.1074/jbc.272.26.16700 |doi-access=free }}
  • {{cite journal | vauthors=McMahon HT, Wigge P, Smith C |title=Clathrin interacts specifically with amphiphysin and is displaced by dynamin. |journal=FEBS Lett. |volume=413 |issue= 2 |pages= 319–22 |year= 1997 |pmid= 9280305 |doi=10.1016/S0014-5793(97)00928-9 |s2cid=42520828 |doi-access= }}
  • {{cite journal | vauthors=Foti M, Mangasarian A, Piguet V |title=Nef-mediated clathrin-coated pit formation. |journal=J. Cell Biol. |volume=139 |issue= 1 |pages= 37–47 |year= 1998 |pmid= 9314527 |doi=10.1083/jcb.139.1.37 | pmc=2139808 |display-authors=etal}}
  • {{cite journal | vauthors=Dell'Angelica EC, Klumperman J, Stoorvogel W, Bonifacino JS |title=Association of the AP-3 adaptor complex with clathrin. |journal=Science |volume=280 |issue= 5362 |pages= 431–4 |year= 1998 |pmid= 9545220 |doi=10.1126/science.280.5362.431 |bibcode=1998Sci...280..431D }}
  • {{cite journal | vauthors=Ramjaun AR, McPherson PS |title=Multiple amphiphysin II splice variants display differential clathrin binding: identification of two distinct clathrin-binding sites. |journal=J. Neurochem. |volume=70 |issue= 6 |pages= 2369–76 |year= 1998 |pmid= 9603201 |doi=10.1046/j.1471-4159.1998.70062369.x |s2cid=21910795 |doi-access=free }}
  • {{cite journal | vauthors=ter Haar E, Musacchio A, Harrison SC, Kirchhausen T |title=Atomic structure of clathrin: a beta propeller terminal domain joins an alpha zigzag linker. |journal=Cell |volume=95 |issue= 4 |pages= 563–73 |year= 1998 |pmid= 9827808 |pmc=4428171 |doi=10.1016/S0092-8674(00)81623-2 }}
  • {{cite journal | vauthors=Laporte SA, Oakley RH, Zhang J |title=The beta2-adrenergic receptor/betaarrestin complex recruits the clathrin adaptor AP-2 during endocytosis. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=96 |issue= 7 |pages= 3712–7 |year= 1999 |pmid= 10097102 |doi=10.1073/pnas.96.7.3712 | pmc=22359 |display-authors=etal|bibcode=1999PNAS...96.3712L|doi-access=free }}
  • {{cite journal | vauthors=Turner CE, Brown MC, Perrotta JA |title=Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankyrin repeat, ARF-GAP protein: A role in cytoskeletal remodeling. |journal=J. Cell Biol. |volume=145 |issue= 4 |pages= 851–63 |year= 1999 |pmid= 10330411 |doi=10.1083/jcb.145.4.851 | pmc=2133183 |display-authors=etal}}
  • {{cite journal | vauthors=Hussain NK, Yamabhai M, Ramjaun AR |title=Splice variants of intersectin are components of the endocytic machinery in neurons and nonneuronal cells. |journal=J. Biol. Chem. |volume=274 |issue= 22 |pages= 15671–7 |year= 1999 |pmid= 10336464 |doi=10.1074/jbc.274.22.15671 |display-authors=etal|doi-access=free }}
  • {{cite journal | vauthors=Ybe JA, Brodsky FM, Hofmann K |title=Clathrin self-assembly is mediated by a tandemly repeated superhelix. |journal=Nature |volume=399 |issue= 6734 |pages= 371–5 |year= 1999 |pmid= 10360576 |doi= 10.1038/20708 |display-authors=etal|bibcode=1999Natur.399..371Y |s2cid=4406014 }}

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External links

  • {{UCSC gene info|CLTC}}

{{PDB Gallery|geneid=1213}}

{{Vesicular transport proteins}}

{{gene-17-stub}}