CDC37
| 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][2]
The protein encoded by this gene is highly similar to Cdc 37, a cell division cycle control protein of Saccharomyces cerevisiae. This protein is a molecular chaperone 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.[11] The central domain is the Hsp90 chaperone (heat shock protein 90) binding domain.[12] The function of the C-terminal domain is unclear.
References
- ^ a b Dai K, Kobayashi R, Beach D (Oct 1996). "Physical interaction of mammalian CDC37 with CDK4". J Biol Chem. 271 (36): 22030–4. doi:10.1074/jbc.271.36.22030. PMID 8703009.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - ^ a b Stepanova L, Leng X, Parker SB, Harper JW (Aug 1996). "Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4". Genes Dev. 10 (12): 1491–502. doi:10.1101/gad.10.12.1491. PMID 8666233.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ "Entrez Gene: CDC37 cell division cycle 37 homolog (S. cerevisiae)".
- ^ Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, McBroom-Cerajewski L, Robinson MD, O'Connor L, Li M, Taylor R, Dharsee M, Ho Y, Heilbut A, Moore L, Zhang S, Ornatsky O, Bukhman YV, Ethier M, Sheng Y, Vasilescu J, Abu-Farha M, Lambert JP, Duewel HS, Stewart II, Kuehl B, Hogue K, Colwill K, Gladwish K, Muskat B, Kinach R, Adams SL, Moran MF, Morin GB, Topaloglou T, Figeys D (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Mol. Syst. Biol. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Lamphere L, Fiore F, Xu X, Brizuela L, Keezer S, Sardet C, Draetta GF, Gyuris J (1997). "Interaction between Cdc37 and Cdk4 in human cells". Oncogene. 14 (16): 1999–2004. doi:10.1038/sj.onc.1201036. PMID 9150368.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, Prodromou C, Pearl LH (2004). "The Mechanism of Hsp90 regulation by the protein kinase-specific cochaperone p50(cdc37)". Cell. 116 (1): 87–98. doi:10.1016/S0092-8674(03)01027-4. PMID 14718169.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Silverstein AM, Grammatikakis N, Cochran BH, Chinkers M, Pratt WB (1998). "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". J. Biol. Chem. 273 (32): 20090–5. doi:10.1074/jbc.273.32.20090. PMID 9685350.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link) - ^ Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ a b Chen G, Cao P, Goeddel DV (2002). "TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90". Mol. Cell. 9 (2): 401–10. doi:10.1016/S1097-2765(02)00450-1. PMID 11864612.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Boudeau J, Deak M, Lawlor MA, Morrice NA, Alessi DR (2003). "Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability". Biochem. J. 370 (Pt 3): 849–57. doi:10.1042/BJ20021813. PMC 1223241. PMID 12489981.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Kimura Y, Rutherford SL, Miyata Y, Yahara I, Freeman BC, Yue L, Morimoto RI, Lindquist S (July 1997). "Cdc37 is a molecular chaperone with specific functions in signal transduction". Genes Dev. 11 (14): 1775–85. doi:10.1101/gad.11.14.1775. PMID 9242486.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ Turnbull EL, Martin IV, Fantes PA (August 2005). "Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90". FEBS J. 272 (16): 4129–40. doi:10.1111/j.1742-4658.2005.04825.x. PMID 16098195.
{{cite journal}}: CS1 maint: multiple names: authors list (link)
Further reading
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