This gene encodes a molecular chaperone that is member of the chaperonin containing TCP1 complex (CCT), also known as the TCP1 ring complex (TRiC). 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 have been observed but have not been thoroughly characterized.[1]
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Nagase T, Miyajima N, Tanaka A, Sazuka T, Seki N, Sato S, Tabata S, Ishikawa K, Kawarabayasi Y, Kotani H (1995). "Prediction of the coding sequences of unidentified human genes. III. The coding sequences of 40 new genes (KIAA0081-KIAA0120) deduced by analysis of cDNA clones from human cell line KG-1". DNA Research. 2 (1): 37–43. doi:10.1093/dnares/2.1.37. PMID7788527.
Kubota H, Hynes G, Carne A, Ashworth A, Willison K (Feb 1994). "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin". Current Biology. 4 (2): 89–99. doi:10.1016/S0960-9822(94)00024-2. PMID7953530.
Yanaka N, Kobayashi K, Wakimoto K, Yamada E, Imahie H, Imai Y, Mori C (May 2000). "Insertional mutation of the murine kisimo locus caused a defect in spermatogenesis". The Journal of Biological Chemistry. 275 (20): 14791–4. doi:10.1074/jbc.C901047199. PMID10747865.
Yoo BC, Kim SH, Cairns N, Fountoulakis M, Lubec G (Jan 2001). "Deranged expression of molecular chaperones in brains of patients with Alzheimer's disease". Biochemical and Biophysical Research Communications. 280 (1): 249–58. doi:10.1006/bbrc.2000.4109. PMID11162507.
Yoo BC, Vlkolinsky R, Engidawork E, Cairns N, Fountoulakis M, Lubec G (Apr 2001). "Differential expression of molecular chaperones in brain of patients with Down syndrome". Electrophoresis. 22 (6): 1233–41. doi:10.1002/1522-2683()22:6<1233::AID-ELPS1233>3.0.CO;2-M. PMID11358150.
Yokota S, Yanagi H, Yura T, Kubota H (Sep 2001). "Cytosolic chaperonin-containing t-complex polypeptide 1 changes the content of a particular subunit species concomitant with substrate binding and folding activities during the cell cycle". European Journal of Biochemistry / FEBS. 268 (17): 4664–73. doi:10.1046/j.1432-1327.2001.02393.x. PMID11532003.
McCormack EA, Llorca O, Carrascosa JL, Valpuesta JM, Willison KR (Aug 2001). "Point mutations in a hinge linking the small and large domains of beta-actin result in trapped folding intermediates bound to cytosolic chaperonin CCT". Journal of Structural Biology. 135 (2): 198–204. doi:10.1006/jsbi.2001.4385. PMID11580269. Check date values in: |year= / |date= mismatch (help)
Llorca O, Martín-Benito J, Gómez-Puertas P, Ritco-Vonsovici M, Willison KR, Carrascosa JL, Valpuesta JM (Aug 2001). "Analysis of the interaction between the eukaryotic chaperonin CCT and its substrates actin and tubulin". Journal of Structural Biology. 135 (2): 205–18. doi:10.1006/jsbi.2001.4359. PMID11580270. Check date values in: |year= / |date= mismatch (help)
Ludwig A, Dietel M, Lage H (2003). "Identification of differentially expressed genes in classical and atypical multidrug-resistant gastric carcinoma cells". Anticancer Research. 22 (6A): 3213–21. PMID12530067.
Imai Y, Soda M, Murakami T, Shoji M, Abe K, Takahashi R (Dec 2003). "A product of the human gene adjacent to parkin is a component of Lewy bodies and suppresses Pael receptor-induced cell death". The Journal of Biological Chemistry. 278 (51): 51901–10. doi:10.1074/jbc.M309655200. PMID14532270. Check date values in: |year= / |date= mismatch (help)
Stelzl U, Worm U, Lalowski M, Haenig C, Brembeck FH, Goehler H, Stroedicke M, Zenkner M, Schoenherr A, Koeppen S, Timm J, Mintzlaff S, Abraham C, Bock N, Kietzmann S, Goedde A, Toksöz E, Droege A, Krobitsch S, Korn B, Birchmeier W, Lehrach H, Wanker EE (Sep 2005). "A human protein-protein interaction network: a resource for annotating the proteome". Cell. 122 (6): 957–68. doi:10.1016/j.cell.2005.08.029. PMID16169070.