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Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37.

Vaughan CK, Mollapour M, Smith JR, Truman A, Hu B, Good VM, Panaretou B, Neckers L, Clarke PA, Workman P, Piper PW, Prodromou C, Pearl LH.

Mol Cell. 2008 Sep 26;31(6):886-95. doi: 10.1016/j.molcel.2008.07.021.


Restricting direct interaction of CDC37 with HSP90 does not compromise chaperoning of client proteins.

Smith JR, de Billy E, Hobbs S, Powers M, Prodromou C, Pearl L, Clarke PA, Workman P.

Oncogene. 2015 Jan 2;34(1):15-26. doi: 10.1038/onc.2013.519. Epub 2013 Dec 2.


Hsp90·Cdc37 Complexes with Protein Kinases Form Cooperatively with Multiple Distinct Interaction Sites.

Eckl JM, Scherr MJ, Freiburger L, Daake MA, Sattler M, Richter K.

J Biol Chem. 2015 Dec 25;290(52):30843-54. doi: 10.1074/jbc.M115.693150. Epub 2015 Oct 28.


ATP-competitive inhibitors block protein kinase recruitment to the Hsp90-Cdc37 system.

Polier S, Samant RS, Clarke PA, Workman P, Prodromou C, Pearl LH.

Nat Chem Biol. 2013 May;9(5):307-12. doi: 10.1038/nchembio.1212. Epub 2013 Mar 17. Erratum in: Nat Chem Biol. 2013 Jun;9(6):406.


Cdc37 interacts with the glycine-rich loop of Hsp90 client kinases.

Terasawa K, Yoshimatsu K, Iemura S, Natsume T, Tanaka K, Minami Y.

Mol Cell Biol. 2006 May;26(9):3378-89.


p50(cdc37) acting in concert with Hsp90 is required for Raf-1 function.

Grammatikakis N, Lin JH, Grammatikakis A, Tsichlis PN, Cochran BH.

Mol Cell Biol. 1999 Mar;19(3):1661-72.


Specific regulation of noncanonical p38alpha activation by Hsp90-Cdc37 chaperone complex in cardiomyocyte.

Ota A, Zhang J, Ping P, Han J, Wang Y.

Circ Res. 2010 Apr 30;106(8):1404-12. doi: 10.1161/CIRCRESAHA.109.213769. Epub 2010 Mar 18.


Cdc37 (cell division cycle 37) restricts Hsp90 (heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites.

Eckl JM, Rutz DA, Haslbeck V, Zierer BK, Reinstein J, Richter K.

J Biol Chem. 2013 May 31;288(22):16032-42. doi: 10.1074/jbc.M112.439257. Epub 2013 Apr 8.


Molecular Mechanism of Protein Kinase Recognition and Sorting by the Hsp90 Kinome-Specific Cochaperone Cdc37.

Keramisanou D, Aboalroub A, Zhang Z, Liu W, Marshall D, Diviney A, Larsen RW, Landgraf R, Gelis I.

Mol Cell. 2016 Apr 21;62(2):260-71. doi: 10.1016/j.molcel.2016.04.005.


Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37.

Shao J, Prince T, Hartson SD, Matts RL.

J Biol Chem. 2003 Oct 3;278(40):38117-20. Epub 2003 Aug 20.


Nucleotide-Free sB-Raf is Preferentially Bound by Hsp90 and Cdc37 In Vitro.

Eckl JM, Daake M, Schwartz S, Richter K.

J Mol Biol. 2016 Oct 9;428(20):4185-4196. doi: 10.1016/j.jmb.2016.09.002. Epub 2016 Sep 13.


Serine/Threonine Kinase Unc-51-like Kinase-1 (Ulk1) Phosphorylates the Co-chaperone Cell Division Cycle Protein 37 (Cdc37) and Thereby Disrupts the Stability of Cdc37 Client Proteins.

Li R, Yuan F, Fu W, Zhang L, Zhang N, Wang Y, Ma K, Li X, Wang L, Zhu WG, Zhao Y.

J Biol Chem. 2017 Feb 17;292(7):2830-2841. doi: 10.1074/jbc.M116.762443. Epub 2017 Jan 10.


Dynamic tyrosine phosphorylation modulates cycling of the HSP90-P50(CDC37)-AHA1 chaperone machine.

Xu W, Mollapour M, Prodromou C, Wang S, Scroggins BT, Palchick Z, Beebe K, Siderius M, Lee MJ, Couvillon A, Trepel JB, Miyata Y, Matts R, Neckers L.

Mol Cell. 2012 Aug 10;47(3):434-43. doi: 10.1016/j.molcel.2012.05.015. Epub 2012 Jun 21.


CK2 binds, phosphorylates, and regulates its pivotal substrate Cdc37, an Hsp90-cochaperone.

Miyata Y, Nishida E.

Mol Cell Biochem. 2005 Jun;274(1-2):171-9.


Phosphorylated and unphosphorylated serine 13 of CDC37 stabilize distinct interactions between its client and HSP90 binding domains.

Liu W, Landgraf R.

Biochemistry. 2015 Feb 24;54(7):1493-504. doi: 10.1021/bi501129g. Epub 2015 Feb 11.


Mammalian p50Cdc37 is a protein kinase-targeting subunit of Hsp90 that binds and stabilizes Cdk4.

Stepanova L, Leng X, Parker SB, Harper JW.

Genes Dev. 1996 Jun 15;10(12):1491-502.


Canonical and kinase activity-independent mechanisms for extracellular signal-regulated kinase 5 (ERK5) nuclear translocation require dissociation of Hsp90 from the ERK5-Cdc37 complex.

Erazo T, Moreno A, Ruiz-Babot G, Rodríguez-Asiain A, Morrice NA, Espadamala J, Bayascas JR, Gómez N, Lizcano JM.

Mol Cell Biol. 2013 Apr;33(8):1671-86. doi: 10.1128/MCB.01246-12. Epub 2013 Feb 19.


The chaperones Hsp90 and Cdc37 mediate the maturation and stabilization of protein kinase C through a conserved PXXP motif in the C-terminal tail.

Gould CM, Kannan N, Taylor SS, Newton AC.

J Biol Chem. 2009 Feb 20;284(8):4921-35. doi: 10.1074/jbc.M808436200. Epub 2008 Dec 17.


Coordinated regulation of serum- and glucocorticoid-inducible kinase 3 by a C-terminal hydrophobic motif and Hsp90-Cdc37 chaperone complex.

Wang Y, Xu W, Zhou D, Neckers L, Chen S.

J Biol Chem. 2014 Feb 21;289(8):4815-26. doi: 10.1074/jbc.M113.518480. Epub 2013 Dec 30.

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