title: The chaperone Hsp90: changing partners for demanding clients.
abstract: The heat shock protein (Hsp)90 chaperone machinery regulates the activity of hundreds of client proteins in the eukaryotic cytosol. It undergoes large conformational changes between states that are similar in energy. These transitions are rate-limiting for the ATPase cycle. It has become evident that several of the many Hsp90 co-chaperones affect the conformational equilibrium by stabilizing specific intermediate states. Consequently, there is an ordered progression of different co-chaperones during the conformational cycle. Asymmetric complexes containing two different co-chaperones may be important for the processing of the client protein, although our understanding of this aspect, as well as the details of the interaction of Hsp90 with client proteins, is still in its infancy.
authors.affiliation: Center for Integrated Protein Science (CIPSM), Department Chemie, Technische Universität München, Lichtenbergstrasse 4, 85747 Garching, Germany.
authors.forename: Alina
authors.initials: A
authors.lastname: Röhl
authors.forename: Julia
authors.initials: J
authors.lastname: Rohrberg
authors.forename: Johannes
authors.initials: J
authors.lastname: Buchner
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D018841:HSP90 Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008958:Models, Molecular; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational
chemical_list: D018841:HSP90 Heat-Shock Proteins; D000255:Adenosine Triphosphate; D000251:Adenosine Triphosphatases