Journal
MOLECULES AND CELLS
Volume 40, Issue 7, Pages 441-449Publisher
KOREAN SOC MOLECULAR & CELLULAR BIOLOGY
DOI: 10.14348/molcells.2017.0115
Keywords
degradation signal (degron); macroautophagy; Nend rule pathway; N-terminal arginylation; proteolysis; protein quality control; ubiquitin code
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Funding
- Basic Science Research Program - Ministry of Science, ICT and Future Planning (MSIP) of Korea [NRF-2016R1A2B3011389]
- Brain Korea 21 PLUS Program
- Seoul National University (SNU) Nobel Laureates Invitation Program
- SNU Hospital
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Proteolysis in eukaryotic cells is mainly mediated by the ubiquitin (Ub)-proteasome system (UPS) and the autophagy-lysosome system (hereafter autophagy). The UPS is a selective proteolytic system in which substrates are recognized and tagged with ubiquitin for processive degradation by the proteasome. Autophagy is a bulk degradative system that uses lysosomal hydrolases to degrade proteins as well as various other cellular constituents. Since the inception of their discoveries, the UPS and autophagy were thought to be independent of each other in components, action mechanisms, and substrate selectivity. Recent studies suggest that cells operate a single proteolytic network comprising of the UPS and autophagy that share notable similarity in many aspects and functionally cooperate with each other to maintain proteostasis. In this review, we discuss the mechanisms underlying the crosstalk and interplay between the UPS and autophagy, with an emphasis on substrate selectivity and compensatory regulation under cellular stresses.
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