Farnesylation of Ydj1 Is Required for In Vivo Interaction with Hsp90 Client Proteins

Identification of the Factors Responsible for the Interaction of Hsp90 and its Client Proteins

Hsp90 is a stress protein that acts as a molecular chaperone and is known to assist in the maturation, folding and stabilization of various cellular proteins known as ‘client proteins’. However, the factors that drive the interaction between Hsp90 and its client proteins are not well understood. In the present investigation, we predicted the basis of the different interaction of Hsp90 with both...

Kdm3a lysine demethylase is an Hsp90 client required for cytoskeletal rearrangements during spermatogenesis

The lysine demethylase Kdm3a (Jhdm2a, Jmjd1a) is required for male fertility, sex determination, and metabolic homeostasis through its nuclear role in chromatin remodeling. Many histone-modifying enzymes have additional nonhistone substrates, as well as nonenzymatic functions, contributing to the full spectrum of events underlying their biological roles. We present two Kdm3a mouse models that e...

Quality control and fate determination of Hsp90 client proteins.

Quality control processes regulate the proteome by determining whether a protein is to be folded or degraded. Hsp90 is a hub in the network of molecular chaperones that maintain this process because it promotes both folding and degradation, in addition to regulating expression of other quality control components. The significance of Hsp90's role in quality control is enhanced by the function of...

Dimerization of Hsp90 is required for in vivo function. Design and analysis of monomers and dimers.

Heat shock protein 90 (Hsp90) plays a central role in signal transduction and has emerged as a promising target for anti-cancer therapeutics, but its molecular mechanism is poorly understood. At physiological concentration, Hsp90 predominantly forms dimers, but the function of full-length monomers in cells is not clear. Hsp90 contains three domains: the N-terminal and middle domains contribute ...

INTERACTION OF PROTEINS WITH SMALL MOLECULES