The Hsp90 chaperone machinery: Conformational dynamics and regulation by co-chaperones

• Published in: Biochimica et biophysica acta Vol. 1823; no. 3; pp. 624 - 635
• Main Authors: Li, Jing, Soroka, Joanna, Buchner, Johannes
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.03.2012
• Subjects: Adenosine Triphosphate - metabolism; Animals; ATPase; Binding Sites; Co-chaperones; Conformational regulation; heat shock proteins; Hsp90 clients; HSP90 Heat-Shock Proteins - chemistry; HSP90 Heat-Shock Proteins - genetics; HSP90 Heat-Shock Proteins - metabolism; Humans; Models, Molecular; Molecular Chaperones - chemistry; Molecular Chaperones - genetics; Molecular Chaperones - metabolism; post-translational modification; Posttranslational modifications; Protein Binding; Protein Conformation; signal transduction; Conformational regulation; Hsp90 clients; Posttranslational modifications; ATPase; Co-chaperones

Hsp90 is a dimeric molecular chaperone required for the activation and stabilization of numerous client proteins many of which are involved in essential cellular processes like signal transduction pathways. This activation process is regulated by ATP-induced large conformational changes, co-chaperon...