CDC37

Hsp90 co-chaperone Cdc37 is a protein that in humans is encoded by the CDC37 gene.[5] This protein is highly similar to Cdc 37, a cell division cycle control protein of Saccharomyces cerevisiae. This protein is a HSP90 Co-chaperone[6] 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.[7]

CDC37
Available structures
PDBOrtholog search: PDBe RCSB
Identifiers
AliasesCDC37, P50cell division cycle 37, cell division cycle 37, HSP90 cochaperone
External IDsOMIM: 605065 MGI: 109531 HomoloGene: 38268 GeneCards: CDC37
Orthologs
SpeciesHumanMouse
Entrez

11140

12539

Ensembl

ENSG00000105401

ENSMUSG00000019471

UniProt

Q16543

Q61081

RefSeq (mRNA)

NM_007065

NM_016742
NM_001378796

RefSeq (protein)

NP_008996

NP_058022
NP_001365725

Location (UCSC)Chr 19: 10.39 – 10.42 MbChr 9: 21.04 – 21.06 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse
Cdc37 N terminal kinase binding
Identifiers
SymbolCDC37_N
PfamPF03234
InterProIPR013855
SCOP21us7 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Cdc37 Hsp90 binding domain
complex of hsp90 and p50
Identifiers
SymbolCDC37_M
PfamPF08565
InterProIPR013874
SCOP21us7 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Cdc37 C terminal domain
complex of hsp90 and p50
Identifiers
SymbolCDC37_C
PfamPF08564
InterProIPR013873
SCOP21us7 / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Interactions

CDC37 has been shown to interact with:

Domain architecture

CDC37 consists of three structural domains. The N-terminal domain binds to protein kinases.[16] The central domain is the Hsp90 chaperone (heat shock protein 90) binding domain.[17] The function of the C-terminal domain is unclear.

References
  1. GRCh38: Ensembl release 89: ENSG00000105401 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000019471 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. Dai K, Kobayashi R, Beach D (September 1996). "Physical interaction of mammalian CDC37 with CDK4". The Journal of Biological Chemistry. 271 (36): 22030–22034. doi:10.1074/jbc.271.36.22030. PMID 8703009.
  6. Mollapour M, Neckers L (March 2012). "Post-translational modifications of Hsp90 and their contributions to chaperone regulation". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research. 1823 (3): 648–655. doi:10.1016/j.bbamcr.2011.07.018. PMC 3226900. PMID 21856339.
  7. "Entrez Gene: CDC37 cell division cycle 37 homolog (S. cerevisiae)".
  8. Stepanova L, Leng X, Parker SB, Harper JW (June 1996). "Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4". Genes & Development. 10 (12): 1491–1502. doi:10.1101/gad.10.12.1491. PMID 8666233.
  9. Ewing RM, Chu P, Elisma F, Li H, Taylor P, Climie S, et al. (2007). "Large-scale mapping of human protein-protein interactions by mass spectrometry". Molecular Systems Biology. 3 (1): 89. doi:10.1038/msb4100134. PMC 1847948. PMID 17353931.
  10. Lamphere L, Fiore F, Xu X, Brizuela L, Keezer S, Sardet C, et al. (April 1997). "Interaction between Cdc37 and Cdk4 in human cells". Oncogene. 14 (16): 1999–2004. doi:10.1038/sj.onc.1201036. PMID 9150368.
  11. Roe SM, Ali MM, Meyer P, Vaughan CK, Panaretou B, Piper PW, et al. (January 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. S2CID 797232.
  12. Silverstein AM, Grammatikakis N, Cochran BH, Chinkers M, Pratt WB (August 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". The Journal of Biological Chemistry. 273 (32): 20090–20095. doi:10.1074/jbc.273.32.20090. PMID 9685350.
  13. Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, et al. (February 2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nature Cell Biology. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216. S2CID 11683986.
  14. Chen G, Cao P, Goeddel DV (February 2002). "TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90". Molecular Cell. 9 (2): 401–410. doi:10.1016/S1097-2765(02)00450-1. PMID 11864612.
  15. Boudeau J, Deak M, Lawlor MA, Morrice NA, Alessi DR (March 2003). "Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability". The Biochemical Journal. 370 (Pt 3): 849–857. doi:10.1042/BJ20021813. PMC 1223241. PMID 12489981.
  16. Kimura Y, Rutherford SL, Miyata Y, Yahara I, Freeman BC, Yue L, et al. (July 1997). "Cdc37 is a molecular chaperone with specific functions in signal transduction". Genes & Development. 11 (14): 1775–1785. doi:10.1101/gad.11.14.1775. PMID 9242486.
  17. Turnbull EL, Martin IV, Fantes PA (August 2005). "Cdc37 maintains cellular viability in Schizosaccharomyces pombe independently of interactions with heat-shock protein 90". The FEBS Journal. 272 (16): 4129–4140. doi:10.1111/j.1742-4658.2005.04825.x. PMID 16098195. S2CID 23442218.

Further reading
This article incorporates text from the public domain Pfam and InterPro: IPR013855
This article incorporates text from the public domain Pfam and InterPro: IPR013874
This article incorporates text from the public domain Pfam and InterPro: IPR013873
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