Dynamic Tyrosine Phosphorylation Modulates Cycling of the HSP90-P50 CDC37-AHA1 Chaperone Machine

Molecular Cell

Volumn 47, Issue 3, 2012, Pages 434-443

  Xu, Wanping ^a   Mollapour, Mehdi ^a   Prodromou, Chrisostomos ^b   Wang, Suiquan ^a   Scroggins, Bradley T ^a   Palchick, Zach ^a   Beebe, Kristin ^a   Siderius, Marco ^c   Lee, Min Jung ^a   Couvillon, Anthony ^d   Trepel, Jane B ^a   Miyata, Yoshihiko ^e   Matts, Robert ^f   Neckers, Len ^a  

^a NATIONAL CANCER INSTITUTE   (United States)

^b UNIVERSITY OF SUSSEX   (United Kingdom)

^c VU UNIVERSITY AMSTERDAM   (Netherlands)

^d CELL SIGNALING TECHNOLOGY   (United States)

^e KYOTO UNIVERSITY   (Japan)

^f OKLAHOMA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; CELL CYCLE PROTEIN 37; CHAPERONE; CHAPERONE AHA1; HEAT SHOCK PROTEIN 90; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CELL CYCLE; CONTROLLED STUDY; HUMAN; HUMAN CELL; NONHUMAN; PROTEIN PHOSPHORYLATION;

ANIMALS; CELL CYCLE PROTEINS; CERCOPITHECUS AETHIOPS; CHAPERONINS; COS CELLS; HSP90 HEAT-SHOCK PROTEINS; HUMANS; MICE; MOLECULAR CHAPERONES; NIH 3T3 CELLS; PHOSPHORYLATION; TYROSINE;

EID: 84864910544     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2012.05.015     Document Type: Article

References (22)

1. Abbas-Terki T., Donzé O., Picard D. The molecular chaperone Cdc37 is required for Ste11 function and pheromone-induced cell cycle arrest. FEBS Lett. 2000, 467:111-116.
2. Fang L., Ricketson D., Getubig L., Darimont B. Unliganded and hormone-bound glucocorticoid receptors interact with distinct hydrophobic sites in the Hsp90 C-terminal domain. Proc. Natl. Acad. Sci. USA 2006, 103:18487-18492.
3. Gilmore T.D., Radke K., Martin G.S. Tyrosine phosphorylation of a 50K cellular polypeptide associated with the Rous sarcoma virus transforming protein pp60src. Mol. Cell. Biol. 1982, 2:199-206.
4. Harst A., Lin H., Obermann W.M. Aha1 competes with Hop, p50 and p23 for binding to the molecular chaperone Hsp90 and contributes to kinase and hormone receptor activation. Biochem. J. 2005, 387:789-796.
5. Koulov A.V., Lapointe P., Lu B., Razvi A., Coppinger J., Dong M.Q., Matteson J., Laister R., Arrowsmith C., Yates J.R., Balch W.E. Biological and structural basis for Aha1 regulation of Hsp90 ATPase activity in maintaining proteostasis in the human disease cystic fibrosis. Mol. Biol. Cell 2010, 21:871-884.
6. Meyer P., Prodromou C., Liao C., Hu B., Mark Roe S., Vaughan C.K., Vlasic I., Panaretou B., Piper P.W., Pearl L.H. Structural basis for recruitment of the ATPase activator Aha1 to the Hsp90 chaperone machinery. EMBO J. 2004, 23:511-519.
7. Miyata Y., Nishida E. CK2 controls multiple protein kinases by phosphorylating a kinase-targeting molecular chaperone, Cdc37. Mol. Cell. Biol. 2004, 24:4065-4074.
8. Miyata Y., Nishida E. Analysis of the CK2-dependent phosphorylation of serine 13 in Cdc37 using a phospho-specific antibody and phospho-affinity gel electrophoresis. FEBS J. 2007, 274:5690-5703.
9. Mollapour M., Neckers L. Post-translational modifications of Hsp90 and their contributions to chaperone regulation. Biochim. Biophys. Acta 2012, 1823:648-655. Published online August 10, 2011. 10.1016/j.bbamcr.2011.07.018.
10. Nathan D.F., Lindquist S. Mutational analysis of Hsp90 function: interactions with a steroid receptor and a protein kinase. Mol. Cell. Biol. 1995, 15:3917-3925.
11. Panaretou B., Siligardi G., Meyer P., Maloney A., Sullivan J.K., Singh S., Millson S.H., Clarke P.A., Naaby-Hansen S., Stein R., et al. Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. Mol. Cell 2002, 10:1307-1318.
12. Ratzke C., Berkemeier F., Hugel T. Heat shock protein 90's mechanochemical cycle is dominated by thermal fluctuations. Proc. Natl. Acad. Sci. USA 2012, 109:161-166. Published online December 19, 2011. 10.1073/pnas.1107930108.
13. Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.M., Polakiewicz R.D., Comb M.J. Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat. Biotechnol. 2005, 23:94-101.
14. Schnaider T., Somogyi J., Csermely P., Szamel M. The Hsp90-specific inhibitor geldanamycin selectively disrupts kinase-mediated signaling events of T-lymphocyte activation. Cell Stress Chaperones 2000, 5:52-61.
15. Sgobba M., Degliesposti G., Ferrari A.M., Rastelli G. Structural models and binding site prediction of the C-terminal domain of human Hsp90: a new target for anticancer drugs. Chem. Biol. Drug Des. 2008, 71:420-433.
16. Shao J., Irwin A., Hartson S.D., Matts R.L. Functional dissection of cdc37: characterization of domain structure and amino acid residues critical for protein kinase binding. Biochemistry 2003, 42:12577-12588.
17. Shao J., Prince T., Hartson S.D., Matts R.L. Phosphorylation of serine 13 is required for the proper function of the Hsp90 co-chaperone, Cdc37. J. Biol. Chem. 2003, 278:38117-38120.
18. Shiau A.K., Harris S.F., Southworth D.R., Agard D.A. Structural Analysis of E. coli hsp90 reveals dramatic nucleotide-dependent conformational rearrangements. Cell 2006, 127:329-340.
19. Siligardi G., Panaretou B., Meyer P., Singh S., Woolfson D.N., Piper P.W., Pearl L.H., Prodromou C. Regulation of Hsp90 ATPase activity by the co-chaperone Cdc37p/p50cdc37. J. Biol. Chem. 2002, 277:20151-20159.
20. Taipale M., Jarosz D.F., Lindquist S. HSP90 at the hub of protein homeostasis: emerging mechanistic insights. Nat. Rev. Mol. Cell Biol. 2010, 11:515-528.
21. Thomas S.M., Brugge J.S. Cellular functions regulated by Src family kinases. Annu. Rev. Cell Dev. Biol. 1997, 13:513-609.
22. Vaughan C.K., Mollapour M., Smith J.R., Truman A., Hu B., Good V.M., Panaretou B., Neckers L., Clarke P.A., Workman P., et al. Hsp90-dependent activation of protein kinases is regulated by chaperone-targeted dephosphorylation of Cdc37. Mol. Cell 2008, 31:886-895.