Biology:CDC37
From HandWiki
Short description: Protein-coding gene in the species Homo sapiens
 Generic protein structure example |
| Cdc37 N terminal kinase binding | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | CDC37_N | ||||||||
| Pfam | PF03234 | ||||||||
| InterPro | IPR013855 | ||||||||
| SCOP2 | 1us7 / SCOPe / SUPFAM | ||||||||
| |||||||||
| Cdc37 Hsp90 binding domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 complex of hsp90 and p50 | |||||||||
| Identifiers | |||||||||
| Symbol | CDC37_M | ||||||||
| Pfam | PF08565 | ||||||||
| InterPro | IPR013874 | ||||||||
| SCOP2 | 1us7 / SCOPe / SUPFAM | ||||||||
| |||||||||
| Cdc37 C terminal domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
complex of hsp90 and p50 | |||||||||
| Identifiers | |||||||||
| Symbol | CDC37_C | ||||||||
| Pfam | PF08564 | ||||||||
| InterPro | IPR013873 | ||||||||
| SCOP2 | 1us7 / SCOPe / SUPFAM | ||||||||
| |||||||||
Hsp90 co-chaperone Cdc37 is a protein that in humans is encoded by the CDC37 gene.[1] This protein is highly similar to Cdc 37, a cell division cycle control protein of Saccharomyces cerevisiae. This protein is a HSP90 Co-chaperone[2] with specific function in cell signal transduction. It has been shown to form complex with Hsp90 and a variety of protein kinases including CDK4, CDK6, SRC, RAF1, MOK, as well as eIF-2 alpha kinases. It is thought to play a critical role in directing Hsp90 to its target kinases.[3]
Interactions
CDC37 has been shown to interact with:
Domain architecture
CDC37 consists of three structural domains. The N-terminal domain binds to protein kinases.[12] The central domain is the Hsp90 chaperone (heat shock protein 90) binding domain.[13] The function of the C-terminal domain is unclear.
References
- ↑ 1.0 1.1 "Physical interaction of mammalian CDC37 with CDK4". The Journal of Biological Chemistry 271 (36): 22030–22034. September 1996. doi:10.1074/jbc.271.36.22030. PMID 8703009.
- ↑ "Post-translational modifications of Hsp90 and their contributions to chaperone regulation". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1823 (3): 648–655. March 2012. doi:10.1016/j.bbamcr.2011.07.018. PMID 21856339.
- ↑ "Entrez Gene: CDC37 cell division cycle 37 homolog (S. cerevisiae)". https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11140.
- ↑ "Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4". Genes & Development 10 (12): 1491–1502. June 1996. doi:10.1101/gad.10.12.1491. PMID 8666233.
- ↑ "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology 3 (1): 89. 2007. doi:10.1038/msb4100134. PMID 17353931.
- ↑ "Interaction between Cdc37 and Cdk4 in human cells". Oncogene 14 (16): 1999–2004. April 1997. doi:10.1038/sj.onc.1201036. PMID 9150368.
- ↑ "The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)". Cell 116 (1): 87–98. January 2004. doi:10.1016/S0092-8674(03)01027-4. PMID 14718169.
- ↑ "p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site". The Journal of Biological Chemistry 273 (32): 20090–20095. August 1998. doi:10.1074/jbc.273.32.20090. PMID 9685350.
- ↑ "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology 6 (2): 97–105. February 2004. doi:10.1038/ncb1086. PMID 14743216.
- ↑ 10.0 10.1 "TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90". Molecular Cell 9 (2): 401–410. February 2002. doi:10.1016/S1097-2765(02)00450-1. PMID 11864612.
- ↑ "Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability". The Biochemical Journal 370 (Pt 3): 849–857. March 2003. doi:10.1042/BJ20021813. PMID 12489981.
- ↑ "Cdc37 is a molecular chaperone with specific functions in signal transduction". Genes & Development 11 (14): 1775–1785. July 1997. doi:10.1101/gad.11.14.1775. PMID 9242486.
- ↑ "Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90". The FEBS Journal 272 (16): 4129–4140. August 2005. doi:10.1111/j.1742-4658.2005.04825.x. PMID 16098195.
Further reading
- "CDC37 is required for p60v-src activity in yeast". Molecular Biology of the Cell 7 (9): 1405–1417. September 1996. doi:10.1091/mbc.7.9.1405. PMID 8885235.
- "Interaction between Cdc37 and Cdk4 in human cells". Oncogene 14 (16): 1999–2004. April 1997. doi:10.1038/sj.onc.1201036. PMID 9150368.
- "Cdc37 is a molecular chaperone with specific functions in signal transduction". Genes & Development 11 (14): 1775–1785. July 1997. doi:10.1101/gad.11.14.1775. PMID 9242486.
- "p50(cdc37) binds directly to the catalytic domain of Raf as well as to a site on hsp90 that is topologically adjacent to the tetratricopeptide repeat binding site". The Journal of Biological Chemistry 273 (32): 20090–20095. August 1998. doi:10.1074/jbc.273.32.20090. PMID 9685350.
- "p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function". Molecular and Cellular Biology 19 (3): 1661–1672. March 1999. doi:10.1128/mcb.19.3.1661. PMID 10022854.
- "Requirement for a kinase-specific chaperone pathway in the production of a Cdk9/cyclin T1 heterodimer responsible for P-TEFb-mediated tat stimulation of HIV-1 transcription". The Journal of Biological Chemistry 275 (1): 279–287. January 2000. doi:10.1074/jbc.275.1.279. PMID 10617616.
- "p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules". Biochemistry 39 (25): 7631–7644. June 2000. doi:10.1021/bi000315r. PMID 10858314.
- "Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinase". The Journal of Biological Chemistry 276 (1): 206–214. January 2001. doi:10.1074/jbc.M007583200. PMID 11036079.
- "DNA cloning using in vitro site-specific recombination". Genome Research 10 (11): 1788–1795. November 2000. doi:10.1101/gr.143000. PMID 11076863.
- "Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor". The Journal of Biological Chemistry 276 (8): 5814–5820. February 2001. doi:10.1074/jbc.M007385200. PMID 11085988.
- "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Reports 1 (3): 287–292. September 2000. doi:10.1093/embo-reports/kvd058. PMID 11256614.
- "Identification and characterization of Harc, a novel Hsp90-associating relative of Cdc37". The Journal of Biological Chemistry 276 (33): 30971–30979. August 2001. doi:10.1074/jbc.M103889200. PMID 11413142.
- "TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90". Molecular Cell 9 (2): 401–410. February 2002. doi:10.1016/S1097-2765(02)00450-1. PMID 11864612.
- "Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37". The Journal of Biological Chemistry 277 (23): 20151–20159. June 2002. doi:10.1074/jbc.M201287200. PMID 11916974.
- "Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function". The Journal of Biological Chemistry 277 (42): 39858–39866. October 2002. doi:10.1074/jbc.M206322200. PMID 12176997.
- "The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically". Biological Chemistry 383 (9): 1335–1342. September 2002. doi:10.1515/BC.2002.152. PMID 12437126.
- "Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability". The Biochemical Journal 370 (Pt 3): 849–857. March 2003. doi:10.1042/BJ20021813. PMID 12489981.
PDB gallery | |
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External links
- Human CDC37 genome location and CDC37 gene details page in the UCSC Genome Browser.
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