BMB Rep. 2016; 49(2): 73-80  
Structure biology of selective autophagy receptors
Byeong-Won Kim, Do Hoon Kwon & Hyun Kyu Song*
Department of Life Sciences, Korea University, Seoul 02841, Korea
Correspondence to: Tel: +82-2-3290-3457; Fax: +82-2-3290-3628; E-mail: hksong@korea.ac.kr
Received: December 18, 2015; Published online: February 28, 2016.
© Korean Society for Biochemistry and Molecular Biology. All rights reserved.

Abstract
Autophagy is a process tightly regulated by various autophagy- related proteins. It is generally classified into non-selective and selective autophagy. Whereas non-selective autophagy is triggered when the cell is under starvation, selective autophagy is involved in eliminating dysfunctional organelles, misfolded and/or ubiquitylated proteins, and intracellular pathogens. These components are recognized by autophagy receptors and delivered to phagophores. Several selective autophagy receptors have been identified and characterized. They usually have some common domains, such as LC3-interacting- region (LIR) motif, a specific cargo interacting (ubiquitin- dependent or ubiquitin-independent) domain. Recently, structural data of these autophagy receptors has been described, which provides an insight of their function in the selective autophagic process. In this review, we summarize the most up-to-date findings about the structure-function of autophagy receptors that regulates selective autophagy.
Keywords: Autophagy, LIR motif, Receptor, Selective autophagy, Ubiquitin binding domain


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