[HTML][HTML] CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation
J Jiang, CA Ballinger, Y Wu, Q Dai, DM Cyr… - Journal of Biological …, 2001 - ASBMB
Proper folding of proteins (either newly synthesized or damaged in response to a stressful
event) occurs in a highly regulated fashion. Cytosolic chaperones such as Hsc/Hsp70 are
assisted by cofactors that modulate the folding machinery in a positive or negative manner.
CHIP (carboxyl terminus ofHsc70-interacting protein) is such a cofactor that interacts with
Hsc70 and, in general, attenuates its most well characterized functions. In addition, CHIP
accelerates ubiquitin-dependent degradation of chaperone substrates. Using an in vitro …
event) occurs in a highly regulated fashion. Cytosolic chaperones such as Hsc/Hsp70 are
assisted by cofactors that modulate the folding machinery in a positive or negative manner.
CHIP (carboxyl terminus ofHsc70-interacting protein) is such a cofactor that interacts with
Hsc70 and, in general, attenuates its most well characterized functions. In addition, CHIP
accelerates ubiquitin-dependent degradation of chaperone substrates. Using an in vitro …