Inhibition of Hsp90: A new strategy for inhibiting protein kinases. Role of molecular chaperones in steroid receptor action. Pratt WB, Galigniana MD, Morishima Y et al. In vivo functions of the Saccharomyces cerevisiae Hsp90 chaperone. This process is experimental and the keywords may be updated as the learning algorithm improves.īuchner J. These keywords were added by machine and not by the authors. The systematic application of large scale approaches to map out the Hsp90 chaperone network should allow the determination of the mechanisms employed by this chaperone system to maintain protein homeostasis in the cell. In yeast Saccharomyces cerevisiae, Hsp90 was shown to interact directly or indirectly with at least 10% of the yeast ORFs. Interaction networks emerging from these large scale efforts clearly demonstrate that Hsp90 plays a central role effecting multiple pathways and cellular processes. Hence, Hsp90 function is highly complex in order to understand that complexity, several groups have attempted to map out the interaction network of this chaperone in yeast and mammalian systems using the latest available proteomic and genomic tools. The functional cycle of the Hsp90 system requires a cohort of cochaperones and cofactors that regulate the activity of this chaperone. In eukaryotes, cytoplasmic Hsp90 is absolutely essential for cell viability under all growth conditions. Hsp90 is an essential and ubiquitous molecular chaperone that is required for the proper folding of a set of client proteins at a late stage in their folding process.
0 kommentar(er)
