Mol. Cells 2017; 40(12): 897~905
Emerging Paradigm of Crosstalk between Autophagy and the Ubiquitin-Proteasome System
Taewook Nam1, Jong Hyun Han1, Sushil Devkota2,*, and Han-Woong Lee1,*
1Department of Biochemistry, College of Life Science and Biotechnology and Yonsei Laboratory Animal Research Center, Yonsei
University, Seoul 03722, Republic of Korea, 2Section of Cell and Developmental Biology, University of California San Diego, La
Jolla, CA, USA
*Correspondence: (HWL); (SD)
Received September 26, 2017; Revised November 13, 2017; Accepted November 23, 2017.; Published online December 12, 2017.
© Korean Society for Molecular and Cellular Biology. All rights reserved.

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Cellular protein homeostasis is maintained by two major degradation pathways, namely the ubiquitin-proteasome system (UPS) and autophagy. Until recently, the UPS and autophagy were considered to be largely independent systems targeting proteins for degradation in the proteasome and lysosome, respectively. However, the identification of crucial roles of molecular players such as ubiquitin and p62 in both of these pathways as well as the observation that blocking the UPS affects autophagy flux and vice versa has generated interest in studying crosstalk between these pathways. Here, we critically review the current understanding of how the UPS and autophagy execute coordinated protein degradation at the molecular level, and shed light on our recent findings indicating an important role of an autophagy-associated transmembrane protein EI24 as a bridging molecule between the UPS and autophagy that functions by regulating the degradation of several E3 ligases with Really Interesting New Gene (RING)- domains.
Keywords: autophagy, crosstalk, EI24, RING-domain, ubiquitin
proteasome system

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