Year: 2011
Type: dissertation
Abstract: Hsp90 is a molecular chaperone modulating the activity of hundreds of client proteins. This activation process is regulated on several levels: by ATP hydrolysis, various specific Hsp90 co-chaperones and posttranslational modifications. In this context, phosphorylation of Hsp90 is of particular importance as there is a conserved phosphatase Ppt1, which specifically associates with Hsp90 and dephosphorylates it. This study allowed identifying in vivo phosphorylation sites of Hsp90 and determining a specific role of Ppt1. In general, phosphorylation down-regulates the Hsp90 machinery by different molecular mechanisms. Sites located in distant regions of Hsp90 affect the ATPase activity, conformational transitions in Hsp90 and co-chaperone binding.
Author: Soroka, Joanna
Language: English
Topic: Heat shock proteins research
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: green
Funder: Technische Universität München
OpenAlex ID: W2750985034