Ontology highlight
ABSTRACT:
SUBMITTER: Mollapour M
PROVIDER: S-EPMC3964875 | biostudies-literature | 2014 Jan
REPOSITORIES: biostudies-literature
Molecular cell 20140101 2
The stability and activity of numerous signaling proteins in both normal and cancer cells depends on the dimeric molecular chaperone heat shock protein 90 (Hsp90). Hsp90's function is coupled to ATP binding and hydrolysis and requires a series of conformational changes that are regulated by cochaperones and numerous posttranslational modifications (PTMs). SUMOylation is one of the least-understood Hsp90 PTMs. Here, we show that asymmetric SUMOylation of a conserved lysine residue in the N domain ...[more]