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DNA Cell Biol. 2013 May;32(5):220-7. doi: 10.1089/dna.2012.1915. Epub 2013 Mar 26.

Interaction domains of p62: a bridge between p62 and selective autophagy.

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  • 1Key Laboratory for Atherosclerology of Hunan Province, Institute of Cardiovascular Disease, University of South China, Hengyang, China.


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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