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  Cdc37 (Cell division dycle 37) restricts Hsp90 (Heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites

Eckl, J. M., Rutz, D. A., Haslbeck, V., Zierer, B. K., Reinstein, J., & Richter, K. (2013). Cdc37 (Cell division dycle 37) restricts Hsp90 (Heat shock protein 90) motility by interaction with N-terminal and middle domain binding sites. Journal of Biological Chemistry, 288(22), 16032-16042. doi:10.1074/jbc.M112.439257.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-9035-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0023-E0A1-0
Genre: Journal Article

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 Creators:
Eckl, Julia M., Author
Rutz, Daniel A., Author
Haslbeck, Veronika, Author
Zierer, Bettina K., Author
Reinstein, Jochen1, Author              
Richter, Klaus, Author
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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 Abstract: he ATPase-driven dimeric molecular Hsp90 (heat shock protein90)anditscofactorCdc37(celldivisioncycle37protein) are crucial to prevent the cellular depletion of many protein kinases. In complex with Hsp90, Cdc37 is thought to bind an important lid structure in the ATPase domain of Hsp90 and inhibit ATP turnover by Hsp90. As different interaction modes havebeenreported,wewereinterestedintheinteractionmech- anism of Hsp90 and Cdc37. We find that Cdc37 can bind to one subunitoftheHsp90dimer.TheinhibitionoftheATPaseactiv- ity is caused by a reduction in the closing rate of Hsp90 without obviously bridging the two subunits or affecting nucleotide accessibility to the binding site. Although human Cdc37 binds to the N-terminal domain of Hsp90, nematodal Cdc37 preferentially interacts with the middle domain of CeHsp90 and hHsp90, expos- ing two Cdc37 interaction sites. A previously unreported site in CeCdc37 is utilized for the middle domain interaction. Dephos- phorylation of CeCdc37 by the Hsp90-associated phosphatase PPH-5, a step required during the kinase activation process, pro- ceeds normally, even if only the new interaction site is used. This shows that the second interaction site is also functionally relevant and highlights that Cdc37, similar to the Hsp90 cofactors Sti1 and Aha1,mayutilizetwodifferentattachmentsitestorestrictthecon- formational freedom and the ATP turnover of Hsp90

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Language(s): eng - English
 Dates: 2012-11-222013-04-082013-04-082013-05-31
 Publication Status: Published in print
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 Rev. Type: Peer
 Identifiers: DOI: 10.1074/jbc.M112.439257
Other: 7916
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Title: Journal of Biological Chemistry
  Other : J. Biol. Chem.
Source Genre: Journal
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Pages: - Volume / Issue: 288 (22) Sequence Number: - Start / End Page: 16032 - 16042 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826