Co-chaperone HSJ1a dually regulates the proteasomal degradation of ataxin-3.
Homo sapiens J domain protein (HSJ1) is a J-domain containing co-chaperone that is known to stimulate ATPase activity of HSP70 chaperone, while it also harbors two ubiquitin (Ub)-interacting motifs (UIMs) that may bind with ubiquitinated substrates and potentially function in protein degradation. We...
Main Authors: | Xue-Chao Gao, Chen-Jie Zhou, Zi-Ren Zhou, Yu-Hang Zhang, Xue-Ming Zheng, Ai-Xin Song, Hong-Yu Hu |
---|---|
Format: | Article |
Language: | English |
Published: |
Public Library of Science (PLoS)
2011-01-01
|
Series: | PLoS ONE |
Online Access: | http://europepmc.org/articles/PMC3098244?pdf=render |
Similar Items
-
PolyQ-expanded proteins impair cellular proteostasis of ataxin-3 through sequestering the co-chaperone HSJ1 into aggregates
by: Hong-Wei Yue, et al.
Published: (2021-04-01) -
Structural transformation of the tandem ubiquitin-interacting motifs in ataxin-3 and their cooperative interactions with ubiquitin chains.
by: Ai-Xin Song, et al.
Published: (2010-10-01) -
Stabilization and Degradation Mechanisms of Cytoplasmic Ataxin-1
by: Mayumi F. Kohiyama, et al.
Published: (2015-01-01) -
Stabilization and Degradation Mechanisms of Cytoplasmic Ataxin-1
by: Mayumi F. Kohiyama, et al.
Published: (2016-05-01) -
HSJ231 - TINJAUN SEJARAH JEPUN APRIL 1994.
by: PPIK, Pusat Pengajian Ilmu Kemanusiaan
Published: (1994)