CDC37

CDC37
Identifiers
AliasesCDC37, P50cell division cycle 37, cell division cycle 37, HSP90 cochaperone
External IDsOMIM: 605065; MGI: 109531; GeneCards: CDC37
Available structures
PDBOrtholog search: PDBe RCSB
Orthologs
DatabasesNCBI: entry; OMA: entry
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:
PDB  IPR013855 PF03234 (ECOD; PDBsum)  
AlphaFold
Cdc37 Hsp90 binding domain
complex of hsp90 and p50
Identifiers
SymbolCDC37_M
PfamPF08565
InterProIPR013874
SCOP21us7 / SCOPe / SUPFAM
Available protein structures:
PDB  IPR013874 PF08565 (ECOD; PDBsum)  
AlphaFold
Cdc37 C terminal domain
complex of hsp90 and p50
Identifiers
SymbolCDC37_C
PfamPF08564
InterProIPR013873
SCOP21us7 / SCOPe / SUPFAM
Available protein structures:
PDB  IPR013873 PF08564 (ECOD; PDBsum)  
AlphaFold

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]

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. ^ a b c GRCh38: Ensembl release 89: ENSG00000105401 – Ensembl, May 2017
  2. ^ a b c 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. ^ a b 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. ^ a b 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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