Post-translational modifications of Hsp90 and translating the chaperone code
Sarah J. Backe, Rebecca Sager, Mark R. Woodford, Alan M. Makedon, Mehdi Mollapour
Abstract
-GlcNAcylation, ubiquitination, and others, toward regulation of Hsp90 function. We also discuss how the Hsp90 modification state affects cellular sensitivity to Hsp90-targeted therapeutics that specifically bind and inhibit its chaperone activity. The ultimate challenge is to decipher the comprehensive and combinatorial array of PTMs that modulate Hsp90 chaperone function, a phenomenon termed the "chaperone code."
Topics & Concepts
Chaperone (clinical)Hsp90Genetic codeComputational biologyPosttranslational modificationChemistryCell biologyBiologyComputer scienceBiochemistryHeat shock proteinDNAMedicineEnzymeGenePathologyHeat shock proteins researchEndoplasmic Reticulum Stress and DiseaseViral Infectious Diseases and Gene Expression in Insects