The complex dance of the molecular chaperone Hsp90
نویسندگان
چکیده
منابع مشابه
Conformational dynamics of the molecular chaperone Hsp90.
The ubiquitous molecular chaperone Hsp90 makes up 1-2% of cytosolic proteins and is required for viability in eukaryotes. Hsp90 affects the folding and activation of a wide variety of substrate proteins including many involved in signaling and regulatory processes. Some of these substrates are implicated in cancer and other diseases, making Hsp90 an attractive drug target. Structural analyses h...
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Hsp90 is an essential molecular chaperone required for the folding and activation of many hundreds of cellular "client" proteins. The ATP-dependent chaperone cycle involves significant conformational rearrangements of the Hsp90 dimer and interaction with a network of cochaperone proteins. Little is known about the mechanism of client protein binding or how cochaperone interactions modulate Hsp9...
متن کاملThe Interaction Network of the Hsp90 Molecular Chaperone
P. Wong · E. R. M. Tillier Department of Medical Biophysics , University of Toronto , Toronto , ON , Canada Abstract Heat shock protein 90 (Hsp 90) is a highly abundant and critical molecular chaperone that plays key roles in cellular quality control systems. The Hsp90 mechanism of function has been the subject of extensive investigation by many groups using traditional biochemical approaches a...
متن کاملThe assembly and intermolecular properties of the hsp70-Hop-hsp90 molecular chaperone complex.
The highly coordinated interactions of several molecular chaperones, including hsp70 and hsp90, are required for the folding and conformational regulation of a variety of proteins in eukaryotic cells, such as steroid hormone receptors and many other signal transduction regulators. The protein called Hop serves as an adaptor protein for hsp70 and hsp90 and is thought to optimize their functional...
متن کاملConformational switching of the molecular chaperone Hsp90 via regulated phosphorylation.
Hsp90 is an essential molecular chaperone in the eukaryotic cytosol. Its function is modulated by cochaperones and posttranslational modifications. Importantly, the phosphatase Ppt1 is a dedicated regulator of the Hsp90 chaperone system. Little is known about Ppt1-dependent phosphorylation sites and how these affect Hsp90 activity. Here, we identified the major phosphorylation sites of yeast Hs...
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ژورنال
عنوان ژورنال: Trends in Biochemical Sciences
سال: 2009
ISSN: 0968-0004
DOI: 10.1016/j.tibs.2009.01.006