4/23/2024 0 Comments 3d comic the chaperone 45![]() ![]() Molecular chaperones are central to proteostasis, as they are involved not only in protein folding but also in degradation 2, 3. Interruption of this process contributes to a variety of pathologies including neurodegenerative disorders and cancer 1. Protein homeostasis, or proteostasis, is the delicate balance of synthesis, folding, trafficking, and degradation of intra- and extracellular proteins. These complexes are inherently flexible, which is important for the ubiquitination process. The 3D structures of the two complexes, obtained using a combination of cryoelectron microscopy and crosslinking mass spectrometry, showed the substrate located between the chaperone and the cochaperone, suggesting a ubiquitination mechanism in which the chaperone-bound substrate is presented to CHIP. Both ternary complexes (Hsp70:p53-TMGST:CHIP and Hsp90:p53-TMGST:CHIP) ubiquitinated the substrate at a higher efficiency than in the absence of the chaperones. We generated complexes between the chaperones (Hsp70 or Hsp90), the cochaperone CHIP and, as substrate, a p53 variant containing the GST protein (p53-TMGST). This is the case for Hsp70 and Hsp90 which, in concert with the cochaperone CHIP, direct their bound substrate to degradation through ubiquitination. ![]() ![]() Some molecular chaperones are involved not only in assisting the folding of proteins but also, given appropriate conditions, in their degradation. ![]()
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