Biology:CCT2 (gene)
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T-complex protein 1 subunit beta is a protein that in humans is encoded by the CCT2 gene.[1][2]
Function
This gene encodes a molecular chaperone that is 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 the gene described in this record have been observed but have not been thoroughly characterized.[2]
Interactions
CCT2 (gene) has been shown to interact with PPP4C.[3][4]
References
- ↑ "Maturation of human cyclin E requires the function of eukaryotic chaperonin CCT". Molecular and Cellular Biology 18 (12): 7584–9. Dec 1998. doi:10.1128/mcb.18.12.7584. PMID 9819444.
- ↑ 2.0 2.1 "Entrez Gene: CCT2 chaperonin containing TCP1, subunit 2 (beta)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=10576.
- ↑ "PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry 283 (43): 29273–84. Oct 2008. doi:10.1074/jbc.M803443200. PMID 18715871.
- ↑ "A novel, evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity". Molecular & Cellular Proteomics 4 (11): 1725–40. Nov 2005. doi:10.1074/mcp.M500231-MCP200. PMID 16085932.
External links
- Human CCT2 genome location and CCT2 gene details page in the UCSC Genome Browser.
- Overview of all the structural information available in the PDB for UniProt: P78371 (T-complex protein 1 subunit beta) at the PDBe-KB.
Further reading
- "Identification of six Tcp-1-related genes encoding divergent subunits of the TCP-1-containing chaperonin". Current Biology 4 (2): 89–99. Feb 1994. doi:10.1016/S0960-9822(94)00024-2. PMID 7953530.
- "3D reconstruction of the ATP-bound form of CCT reveals the asymmetric folding conformation of a type II chaperonin". Nature Structural Biology 6 (7): 639–42. Jul 1999. doi:10.1038/10689. PMID 10404219.
- "Individual subunits of the eukaryotic cytosolic chaperonin mediate interactions with binding sites located on subdomains of beta-actin". The Journal of Biological Chemistry 275 (25): 18985–94. Jun 2000. doi:10.1074/jbc.M910297199. PMID 10748209.
- "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. Sep 2001. doi:10.1046/j.1432-1327.2001.02393.x. PMID 11532003.
- "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. Aug 2001. doi:10.1006/jsbi.2001.4385. PMID 11580269.
- "Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides". Nature Biotechnology 21 (5): 566–9. May 2003. doi:10.1038/nbt810. PMID 12665801.
- "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. Dec 2003. doi:10.1074/jbc.M309655200. PMID 14532270.
- "Proteomic, functional, and domain-based analysis of in vivo 14-3-3 binding proteins involved in cytoskeletal regulation and cellular organization". Current Biology 14 (16): 1436–50. Aug 2004. doi:10.1016/j.cub.2004.07.051. PMID 15324660.
- "Nucleolar proteome dynamics". Nature 433 (7021): 77–83. Jan 2005. doi:10.1038/nature03207. PMID 15635413.
- "Proteomic analysis of SUMO4 substrates in HEK293 cells under serum starvation-induced stress". Biochemical and Biophysical Research Communications 337 (4): 1308–18. Dec 2005. doi:10.1016/j.bbrc.2005.09.191. PMID 16236267.
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