The Interaction Network of the Hsp90 Molecular Chaperone

Heat shock protein (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 as well as high-throughput methods, however, the Hsp90 functional cycle still remains enigmatic. A complicating factor in understanding Hsp90 function is the presence of many cofactors and co-chaperones that assist in Hsp90 chaperoning activity. The widely used model organism, Saccharomyces cerevisiae (budding yeast), contains two highly conserved members of the Hsp90 family, Hsp82, and Hsc82, and has been used as a model organism for mapping Hsp90 interactors. High-throughput proteomic studies on the yeast Hsp90 provided a wealth of information from a global perspective. More recently, such studies in mammalian cells have led to a better understanding of Hsp90 function. Here, we discuss the Hsp90 functions and highlight the most recent efforts leading to the construction of the Hsp90 interaction networks.