期刊
DNA AND CELL BIOLOGY
卷 32, 期 5, 页码 220-227出版社
MARY ANN LIEBERT, INC
DOI: 10.1089/dna.2012.1915
关键词
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资金
- Innovative Research Team for Science and Technology in Higher Educational Institutions of Hunan Province
- Natural Science Foundation of China [81070221]
- Visiting Scholar Foundation of Key Laboratory for Biorheological Science and Technology (Chongqing University) of Ministry of Education
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 domains have been found to be linked to ubiquitinated protein degradation by autophagy. Therefore, understanding the functional domains of p62 is important. In this review, we attempt to expound the mechanism of connection between p62 and selective autophagy to illustrate how the domains of p62 regulate selective autophagy, and to provide a new direction and perspective on selective autophagy research.
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