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• W2590312535 abstract "The ability of Hsp90 to activate a disparate clientele implicates this chaperone in diverse biological processes. To accommodate such varied roles, Hsp90 requires a variety of regulatory mechanisms that are coordinated in order to modulate its activity appropriately. Amongst these, the master-regulator heat shock factor 1 (HSF1) is critically important in upregulating Hsp90 during stress, but is also responsible, through interaction with specific transcription factors (such as STAT1 and Strap/p300) for the integration of a variety of biological signals that ultimately modulate Hsp90 expression. Additionally, transcription factors, such as STAT1, STAT3 (including STAT1-STAT3 oligomers), NF-IL6, and NF-kB, are known to influence Hsp90 expression directly. Co-chaperones offer another mechanism for Hsp90 regulation, and these can modulate the chaperone cycle appropriately for specific clientele. Co-chaperones include those that deliver specific clients to Hsp90, and others that regulate the chaperone cycle for specific Hsp90-client complexes by modulating Hsp90s ATPase activity. Finally, post-translational modification (PTM) of Hsp90 and its co-chaperones helps too further regulate the variety of different Hsp90 complexes found in cells." @default.
• W2590312535 created "2017-03-03" @default.
• W2590312535 creator A5050346032 @default.
• W2590312535 date "2017-01-01" @default.
• W2590312535 modified "2023-10-16" @default.
• W2590312535 title "Regulatory Mechanisms of Hsp90" @default.
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• W2590312535 doi "https://doi.org/10.21767/2471-8084.100030" @default.
• W2590312535 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5346293" @default.
• W2590312535 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28289734" @default.
• W2590312535 hasPublicationYear "2017" @default.
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