2009
DOI: 10.1038/embor.2009.153
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Hsp90 is regulated by a switch point in the C‐terminal domain

Abstract: Heat shock protein 90 (Hsp90) is an abundant, dimeric ATPdependent molecular chaperone, and ATPase activity is essential for its in vivo functions. S-nitrosylation of a residue located in the carboxy-terminal domain has been shown to affect Hsp90 activity in vivo. To understand how variation of a specific amino acid far away from the amino-terminal ATP-binding site regulates Hsp90 functions, we mutated the corresponding residue and analysed yeast and human Hsp90 variants both in vivo and in vitro. Here, we sho… Show more

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Cited by 153 publications
(156 citation statements)
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“…We saw that the heme-independent sGC activator BAY 60-2770 could mimic the effect of NO in promoting hsp90 dissociation, whereas the heme-dependent sGC activator BAY 41-2272 could not. The ability of BAY 60-2770 to do so is perhaps the best indicator that the mechanism of NO action does not necessarily require any NO-based protein modifications such as protein S-nitrosation or tyrosine nitration, which can otherwise occur in hsp90 and sGC proteins when cells are exposed to NO (23)(24)(25). Rather, our results suggest a mechanism of action that involves fundamental changes in the apo-sGC-␤1 subunit.…”
Section: Discussionmentioning
confidence: 70%
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“…We saw that the heme-independent sGC activator BAY 60-2770 could mimic the effect of NO in promoting hsp90 dissociation, whereas the heme-dependent sGC activator BAY 41-2272 could not. The ability of BAY 60-2770 to do so is perhaps the best indicator that the mechanism of NO action does not necessarily require any NO-based protein modifications such as protein S-nitrosation or tyrosine nitration, which can otherwise occur in hsp90 and sGC proteins when cells are exposed to NO (23)(24)(25). Rather, our results suggest a mechanism of action that involves fundamental changes in the apo-sGC-␤1 subunit.…”
Section: Discussionmentioning
confidence: 70%
“…3, B and E). In particular, there emerged a lower M r subpopulation of sGC-␤1 that clearly had no hsp90 associated with it (lanes [23][24][25][26]. This subpopulation existed only transiently in the cells because it was no longer present in cells that underwent a longer SNAP exposure for 30 min (Fig.…”
Section: E and F)mentioning
confidence: 96%
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“…Expression Vectors and Transfection-pcDNA3.1/FLAG/ HSP90␣ was provided by Dr. Johannes Buchner (Technische Universität München, Department Chemie, LS Biotechnologie, München, Germany) (32). The EGFP-AKR1B10 vector has been produced previously (14).…”
Section: Methodsmentioning
confidence: 99%
“…Also, phosphorylation at Thr22 by casein kinase 2 modulates Hsp90 interactions with the cochaperones Cdc37 and Aha1 65 . In addition, yeast Hsp90 is S-nitrosylated, which affects its dimerization dynamics and activity 68 , and by analogy with its mammalian counterpart 69 , yeast Hsp90 might also be acetylated.…”
Section: Post-translational Modification Of Hsp90mentioning
confidence: 99%