CDC37

CDC37

Cell division cycle 37 homolog (S. cerevisiae), also known as CDC37, is a human gene.

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.cite web | title = Entrez Gene: CDC37 cell division cycle 37 homolog (S. cerevisiae)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=11140| accessdate = ]

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Stepanova L, Leng X, Parker SB, Harper JW |title=Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4. |journal=Genes Dev. |volume=10 |issue= 12 |pages= 1491–502 |year= 1996 |pmid= 8666233 |doi=
*cite journal | author=Dai K, Kobayashi R, Beach D |title=Physical interaction of mammalian CDC37 with CDK4. |journal=J. Biol. Chem. |volume=271 |issue= 36 |pages= 22030–4 |year= 1996 |pmid= 8703009 |doi=
*cite journal | author=Dey B, Lightbody JJ, Boschelli F |title=CDC37 is required for p60v-src activity in yeast. |journal=Mol. Biol. Cell |volume=7 |issue= 9 |pages= 1405–17 |year= 1997 |pmid= 8885235 |doi=
*cite journal | author=Lamphere L, Fiore F, Xu X, "et al." |title=Interaction between Cdc37 and Cdk4 in human cells. |journal=Oncogene |volume=14 |issue= 16 |pages= 1999–2004 |year= 1997 |pmid= 9150368 |doi= 10.1038/sj.onc.1201036
*cite journal | author=Kimura Y, Rutherford SL, Miyata Y, "et al." |title=Cdc37 is a molecular chaperone with specific functions in signal transduction. |journal=Genes Dev. |volume=11 |issue= 14 |pages= 1775–85 |year= 1997 |pmid= 9242486 |doi=
*cite journal | author=Silverstein AM, Grammatikakis N, Cochran BH, "et al." |title=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. |journal=J. Biol. Chem. |volume=273 |issue= 32 |pages= 20090–5 |year= 1998 |pmid= 9685350 |doi=
*cite journal | author=Grammatikakis N, Lin JH, Grammatikakis A, "et al." |title=p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function. |journal=Mol. Cell. Biol. |volume=19 |issue= 3 |pages= 1661–72 |year= 1999 |pmid= 10022854 |doi=
*cite journal | author=O'Keeffe B, Fong Y, Chen D, "et al." |title=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. |journal=J. Biol. Chem. |volume=275 |issue= 1 |pages= 279–87 |year= 2000 |pmid= 10617616 |doi=
*cite journal | author=Hartson SD, Irwin AD, Shao J, "et al." |title=p50(cdc37) is a nonexclusive Hsp90 cohort which participates intimately in Hsp90-mediated folding of immature kinase molecules. |journal=Biochemistry |volume=39 |issue= 25 |pages= 7631–44 |year= 2000 |pmid= 10858314 |doi=
*cite journal | author=Shao J, Grammatikakis N, Scroggins BT, "et al." |title=Hsp90 regulates p50(cdc37) function during the biogenesis of the activeconformation of the heme-regulated eIF2 alpha kinase. |journal=J. Biol. Chem. |volume=276 |issue= 1 |pages= 206–14 |year= 2001 |pmid= 11036079 |doi= 10.1074/jbc.M007583200
*cite journal | author=Hartley JL, Temple GF, Brasch MA |title=DNA cloning using in vitro site-specific recombination. |journal=Genome Res. |volume=10 |issue= 11 |pages= 1788–95 |year= 2001 |pmid= 11076863 |doi=
*cite journal | author=Rao J, Lee P, Benzeno S, "et al." |title=Functional interaction of human Cdc37 with the androgen receptor but not with the glucocorticoid receptor. |journal=J. Biol. Chem. |volume=276 |issue= 8 |pages= 5814–20 |year= 2001 |pmid= 11085988 |doi= 10.1074/jbc.M007385200
*cite journal | author=Simpson JC, Wellenreuther R, Poustka A, "et al." |title=Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing. |journal=EMBO Rep. |volume=1 |issue= 3 |pages= 287–92 |year= 2001 |pmid= 11256614 |doi= 10.1093/embo-reports/kvd058
*cite journal | author=Scholz GM, Cartledge K, Hall NE |title=Identification and characterization of Harc, a novel Hsp90-associating relative of Cdc37. |journal=J. Biol. Chem. |volume=276 |issue= 33 |pages= 30971–9 |year= 2001 |pmid= 11413142 |doi= 10.1074/jbc.M103889200
*cite journal | author=Chen G, Cao P, Goeddel DV |title=TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90. |journal=Mol. Cell |volume=9 |issue= 2 |pages= 401–10 |year= 2002 |pmid= 11864612 |doi=
*cite journal | author=Siligardi G, Panaretou B, Meyer P, "et al." |title=Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. |journal=J. Biol. Chem. |volume=277 |issue= 23 |pages= 20151–9 |year= 2002 |pmid= 11916974 |doi= 10.1074/jbc.M201287200
*cite journal | author=Basso AD, Solit DB, Chiosis G, "et al." |title=Akt forms an intracellular complex with heat shock protein 90 (Hsp90) and Cdc37 and is destabilized by inhibitors of Hsp90 function. |journal=J. Biol. Chem. |volume=277 |issue= 42 |pages= 39858–66 |year= 2002 |pmid= 12176997 |doi= 10.1074/jbc.M206322200
*cite journal | author=Abbas-Terki T, Briand PA, Donzé O, Picard D |title=The Hsp90 co-chaperones Cdc37 and Sti1 interact physically and genetically. |journal=Biol. Chem. |volume=383 |issue= 9 |pages= 1335–42 |year= 2003 |pmid= 12437126 |doi=
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Boudeau J, Deak M, Lawlor MA, "et al." |title=Heat-shock protein 90 and Cdc37 interact with LKB1 and regulate its stability. |journal=Biochem. J. |volume=370 |issue= Pt 3 |pages= 849–57 |year= 2003 |pmid= 12489981 |doi= 10.1042/BJ20021813

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