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Interaction domains of p62: A bridge between p62 and selective autophagy

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成果类型:
期刊论文
作者:
Lin, Xiaolong;Li, Shuang;Zhao, Yue;Ma, Xiaofeng;Zhang, Kai;...
通讯作者:
Wang, Zuo
作者机构:
[Zhao, Yue; Ma, Xiaofeng; Li, Shuang; He, Xinglan; Wang, Zuo; Zhang, Kai; Lin, Xiaolong] Univ South China, Inst Cardiovasc Dis, Key Lab Atherosclerol Hunan Prov, Hengyang 421001, Peoples R China.
通讯机构:
[Wang, Zuo] U
Univ South China, Inst Cardiovasc Dis, Key Lab Atherosclerol Hunan Prov, Hengyang 421001, Peoples R China.
语种:
英文
关键词:
Autophagy
期刊:
DNA AND CELL BIOLOGY
ISSN:
1044-5498
年:
2013
卷:
32
期:
5
页码:
220-227
基金类别:
Innovative Research Team for Science and Technology in Higher Educational Institutions of Hunan Province; Natural Science Foundation of ChinaNational Natural Science Foundation of China (NSFC) [81070221]; Visiting Scholar Foundation of Key Laboratory for Biorheological Science and Technology (Chongqing University) of Ministry of Education
机构署名:
本校为第一且通讯机构
院系归属:
医学院
摘要:
p62 is a multidomain protein that contains different kinds of protein-protein interaction domains, including an N-terminal PB1 domain, a ZZ-type zinc finger domain, a nuclear localization signal (NLS), an export motif (NES), the LC3-interacting region (LIR), the KEAP1-interacting region (KIR), and a C-terminal Ub-associated domain (UBA). p62 is involved in the degradation of protein aggregates and cytoplasmic bodies via selective autophagy through its PB1, LIR, and UBA domains to maintain homeostasis in the cell. Moreover, NES, NLS, KIR, and ZZ...

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