In humans, the geneT-complex 1, a.k.a. TCP1, encodes the proteinTCP-1[a], a.k.a. T-complex protein 1 subunit alpha.[5][6][7]
Function
This gene encodes a molecular chaperone that is a member of the TRiC complex. This complex consists of two identical stacked rings, each containing eight different proteins. Unfolded polypeptides enter the central cavity of the complex and are folded in an ATP-dependent manner. The complex folds various proteins, including actin and tubulin. Alternate transcriptional splice variants of this gene, encoding different isoforms, have been characterized.[7]
Interactions
T-complex 1 has been shown to interact with PPP4C[8][9] and HDAC3.[10] CCT also directly interacts with lectin type oxidized LDL receptor-1 (LOX-1) while its ligand oxidized low density lipoprotein (OxLDL) disassociates CCT from LOX-1.[11]
Notes
^The term "TCP-1" is variously expanded as "T-complex protein 1" and "tailless complex polypeptide 1". The "T-complex" is the same as tailless complex, a CCT locus associated with tail length in mice.
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Fonatsch C, Gradl G, Ragoussis J, Ziegler A (Oct 1987). "Assignment of the TCP1 locus to the long arm of human chromosome 6 by in situ hybridization". Cytogenet Cell Genet. 45 (2): 109–12. doi:10.1159/000132439. PMID3476253.
Horwich AL, Willison KR (1993). "Protein folding in the cell: functions of two families of molecular chaperone, hsp 60 and TF55-TCP1". Philos. Trans. R. Soc. Lond. B Biol. Sci. 339 (1289): 313–25, discussion 325–6. doi:10.1098/rstb.1993.0030. PMID8098536.
Burston SG, Clarke AR (1997). "Molecular chaperones: physical and mechanistic properties". Essays Biochem. 29: 125–36. PMID9189717.
Blanché H, Wright LG, Vergnaud G, de Gouyon B, Lauthier V, Silver LM, Dausset J, Cann HM, Spielman RS (1992). "Genetic mapping of three human homologues of murine t-complex genes localizes TCP10 to 6q27, 15 cM distal to TCP1 and PLG". Genomics. 12 (4): 826–8. doi:10.1016/0888-7543(92)90317-L. PMID1572657.
Dawson SJ, White LA (1992). "Treatment of Haemophilus aphrophilus endocarditis with ciprofloxacin". J. Infect. 24 (3): 317–20. doi:10.1016/S0163-4453(05)80037-4. PMID1602151.
Roobol A, Holmes FE, Hayes NV, Baines AJ, Carden MJ (1995). "Cytoplasmic chaperonin complexes enter neurites developing in vitro and differ in subunit composition within single cells". J. Cell Sci. 108 (4): 1477–88. doi:10.1242/jcs.108.4.1477. PMID7615668.
Ashworth A (1994). "Two acetyl-CoA acetyltransferase genes located in the t-complex region of mouse chromosome 17 partially overlap the Tcp-1 and Tcp-1x genes". Genomics. 18 (2): 195–8. doi:10.1006/geno.1993.1454. PMID7904580.
Kubota H, Hynes G, Carne A, Ashworth A, Willison K (1994). "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin". Curr. Biol. 4 (2): 89–99. doi:10.1016/S0960-9822(94)00024-2. PMID7953530. S2CID31300131.
Moudjou M, Bordes N, Paintrand M, Bornens M (1996). "gamma-Tubulin in mammalian cells: the centrosomal and the cytosolic forms". J. Cell Sci. 109 (4): 875–87. doi:10.1242/jcs.109.4.875. PMID8718679.
Masuno M, Fukao T, Song XQ, Yamaguchi S, Orii T, Kondo N, Imaizumi K, Kuroki Y (1997). "Assignment of the human cytosolic acetoacetyl-coenzyme A thiolase (ACAT2) gene to chromosome 6q25.3-q26". Genomics. 36 (1): 217–8. doi:10.1006/geno.1996.0452. PMID8812443.
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