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*{{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  }}
*{{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  }}
*{{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=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  }}
*{{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  }}
*{{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  }}
*{{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 |doi=10.1016/S0092-8674(00)81623-2  }}
*{{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 |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}}
*{{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}}
*{{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=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}}
*{{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}}
*{{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}}
*{{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 }}
}}
}}
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Latest revision as of 01:16, 23 June 2018

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Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

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

  1. 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.
  2. 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.
  3. "Entrez Gene: CLTC clathrin, heavy chain (Hc)".
  4. 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.
  5. 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

External links

This article incorporates text from the United States National Library of Medicine, which is in the public domain.