CLTC

Revision as of 15:08, 4 September 2012 by WikiBot (talk | contribs) (Robot: Automated text replacement (-{{WikiDoc Cardiology Network Infobox}} +, -<references /> +{{reflist|2}}, -{{reflist}} +{{reflist|2}}))
(diff) ← Older revision | Latest revision (diff) | Newer revision → (diff)
Jump to navigation Jump to search


Clathrin, heavy chain (Hc)
PDB rendering based on 1b89.
Available structures
PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB
Identifiers
Symbols CLTC ; CHC17; CLH-17; CLTCL2; Hc; KIAA0034
External IDs Template:OMIM5 Template:MGI HomoloGene3572
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species Human Mouse
Entrez n/a n/a
Ensembl n/a n/a
UniProt n/a n/a
RefSeq (mRNA) n/a n/a
RefSeq (protein) n/a n/a
Location (UCSC) n/a n/a
PubMed search n/a n/a

Clathrin, heavy chain (Hc), also known as CLTC, is a human gene.

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.[1]


See also

References

  1. "Entrez Gene: CLTC clathrin, heavy chain (Hc)".

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.
  • Dodge GR, Kovalszky I, McBride OW; et al. (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. PMID 1765375.
  • 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". DNA Res. 1 (1): 27–35. PMID 7584026.
  • 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. 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. 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. 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. 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. PMID 9280305.
  • Foti M, Mangasarian A, Piguet V; et al. (1998). "Nef-mediated clathrin-coated pit formation". J. Cell Biol. 139 (1): 37–47. 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. 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. 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. 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. 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. 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. 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.

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

Template:WikiDoc Sources