TY - JOUR
T1 - Endoplasmic reticulum protein quality control is determined by cooperative interactions between Hsp/c70 protein and the CHIP E3 ligase
AU - Matsumura, Yoshihiro
AU - Sakai, Juro
AU - Skach, William R.
PY - 2013/10/25
Y1 - 2013/10/25
N2 - Background: The CHIP E3 ligase regulates Hsp70 pro-degradation activities. Results: The P269A CHIP U-box mutation induces CHIP oligomerization and modulates nucleotide- and substrate-dependent interactions between the TPR domain and Hsp70 C terminus. Conclusion: The U-box domain plays a key role in CHIP recruitment to Hsp70-client complexes, possibly by controlling oligomerization. Significance: Hsp70-CHIP substrate triage is governed by complex allosteric interactions between multiple domains in both proteins.
AB - Background: The CHIP E3 ligase regulates Hsp70 pro-degradation activities. Results: The P269A CHIP U-box mutation induces CHIP oligomerization and modulates nucleotide- and substrate-dependent interactions between the TPR domain and Hsp70 C terminus. Conclusion: The U-box domain plays a key role in CHIP recruitment to Hsp70-client complexes, possibly by controlling oligomerization. Significance: Hsp70-CHIP substrate triage is governed by complex allosteric interactions between multiple domains in both proteins.
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U2 - 10.1074/jbc.M113.479345
DO - 10.1074/jbc.M113.479345
M3 - Article
C2 - 23990462
AN - SCOPUS:84886649071
VL - 288
SP - 31069
EP - 31079
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 43
ER -