Literature DB >> 29177662

Detecting Posttranslational Modifications of Hsp90.

Rebecca A Sager1,2,3, Mark R Woodford1,2, Len Neckers4, Mehdi Mollapour5,6,7.   

Abstract

The molecular chaperone Heat Shock Protein 90 (Hsp90) is essential in eukaryotes. Hsp90 chaperones proteins that are important determinants of multistep carcinogenesis. The chaperone function of Hsp90 is linked to its ability to bind and hydrolyze ATP. Co-chaperones as well as posttranslational modifications (phosphorylation, SUMOylation, and ubiquitination) are important for its stability and regulation of the ATPase activity. Both mammalian and yeast cells can be used to express and purify Hsp90 and also detect its posttranslational modifications by immunoblotting.

Entities:  

Keywords:  Heat shock protein 90 (Hsp90); Molecular chaperones; Phosphorylation; Posttranslational modification; SUMOylation; Ubiquitination

Mesh:

Substances:

Year:  2018        PMID: 29177662      PMCID: PMC6376113          DOI: 10.1007/978-1-4939-7477-1_16

Source DB:  PubMed          Journal:  Methods Mol Biol        ISSN: 1064-3745


  52 in total

1.  The importance of ATP binding and hydrolysis by hsp90 in formation and function of protein heterocomplexes.

Authors:  J P Grenert; B D Johnson; D O Toft
Journal:  J Biol Chem       Date:  1999-06-18       Impact factor: 5.157

2.  Phosphorylation and oligomerization states of native pig brain HSP90 studied by mass spectrometry.

Authors:  C Garnier; D Lafitte; T J Jorgensen; O N Jensen; C Briand; V Peyrot
Journal:  Eur J Biochem       Date:  2001-04

3.  Cpr6 and Cpr7, two closely related Hsp90-associated immunophilins from Saccharomyces cerevisiae, differ in their functional properties.

Authors:  C Mayr; K Richter; H Lilie; J Buchner
Journal:  J Biol Chem       Date:  2000-11-03       Impact factor: 5.157

4.  Hsp90 phosphorylation is linked to its chaperoning function. Assembly of the reovirus cell attachment protein.

Authors:  Y G Zhao; R Gilmore; G Leone; M C Coffey; B Weber; P W Lee
Journal:  J Biol Chem       Date:  2001-07-03       Impact factor: 5.157

5.  Domain mapping studies reveal that the M domain of hsp90 serves as a molecular scaffold to regulate Akt-dependent phosphorylation of endothelial nitric oxide synthase and NO release.

Authors:  Jason Fontana; David Fulton; Yan Chen; Todd A Fairchild; Timothy J McCabe; Naoya Fujita; Takashi Tsuruo; William C Sessa
Journal:  Circ Res       Date:  2002-05-03       Impact factor: 17.367

6.  Phosphorylation and hsp90 binding mediate heat shock stabilization of p53.

Authors:  Chuangui Wang; Jiandong Chen
Journal:  J Biol Chem       Date:  2002-11-08       Impact factor: 5.157

7.  Sti1 is a non-competitive inhibitor of the Hsp90 ATPase. Binding prevents the N-terminal dimerization reaction during the atpase cycle.

Authors:  Klaus Richter; Paul Muschler; Otmar Hainzl; Jochen Reinstein; Johannes Buchner
Journal:  J Biol Chem       Date:  2003-01-13       Impact factor: 5.157

8.  Aha1 binds to the middle domain of Hsp90, contributes to client protein activation, and stimulates the ATPase activity of the molecular chaperone.

Authors:  Gregor P Lotz; Hongying Lin; Anja Harst; Wolfgang M J Obermann
Journal:  J Biol Chem       Date:  2003-02-24       Impact factor: 5.157

9.  Tyrosine phosphorylation of HSP90 within the P2X7 receptor complex negatively regulates P2X7 receptors.

Authors:  Elena Adinolfi; Miran Kim; Mark T Young; Francesco Di Virgilio; Annmarie Surprenant
Journal:  J Biol Chem       Date:  2003-07-17       Impact factor: 5.157

10.  Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1.

Authors:  Barry Panaretou; Giuliano Siligardi; Philippe Meyer; Alison Maloney; Janis K Sullivan; Shradha Singh; Stefan H Millson; Paul A Clarke; Soren Naaby-Hansen; Rob Stein; Rainer Cramer; Mehdi Mollapour; Paul Workman; Peter W Piper; Laurence H Pearl; Chrisostomos Prodromou
Journal:  Mol Cell       Date:  2002-12       Impact factor: 17.970

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  4 in total

Review 1.  Post-translational modifications of Hsp90 and translating the chaperone code.

Authors:  Sarah J Backe; Rebecca A Sager; Mark R Woodford; Alan M Makedon; Mehdi Mollapour
Journal:  J Biol Chem       Date:  2020-06-11       Impact factor: 5.157

Review 2.  Not quite the SSAme: unique roles for the yeast cytosolic Hsp70s.

Authors:  Sarah K Lotz; Laura E Knighton; Gary W Jones; Andrew W Truman
Journal:  Curr Genet       Date:  2019-04-24       Impact factor: 3.886

3.  Post-translational Regulation of FNIP1 Creates a Rheostat for the Molecular Chaperone Hsp90.

Authors:  Rebecca A Sager; Mark R Woodford; Sarah J Backe; Alan M Makedon; Alexander J Baker-Williams; Bryanna T DiGregorio; David R Loiselle; Timothy A Haystead; Natasha E Zachara; Chrisostomos Prodromou; Dimitra Bourboulia; Laura S Schmidt; W Marston Linehan; Gennady Bratslavsky; Mehdi Mollapour
Journal:  Cell Rep       Date:  2019-01-29       Impact factor: 9.423

Review 4.  Inhibitors of HSP90 in melanoma.

Authors:  Aleksandra Mielczarek-Lewandowska; Mariusz L Hartman; Malgorzata Czyz
Journal:  Apoptosis       Date:  2020-02       Impact factor: 4.677

  4 in total

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