The Role of Ubiquitylation and SUMOylation in Autophagy
Sushil Devkota
from: SUMOylation and Ubiquitination: Current and Emerging Concepts (Edited by: Van G. Wilson). Caister Academic Press, U.K. (2019) Pages: 349-362.
Abstract
Post-translational modifications such as ubiquitination and sumoylation are central players in determining the fates of proteins by providing specificity to mediate their degradation or alteration of functions. Ubiquitin is the central molecule in the ubiquitin-proteasome system (UPS), which works by tagging the proteins to be degraded with polyubiquitin chains, a mark identified by the barrel-shaped proteasome as an 'eat-me' signal. Autophagy, on the other hand, is a vesicular trafficking system specialized in degrading larger cargos and long-lived proteins in the lysosome. Until recently, autophagy and UPS were considered separate protein degradation machineries owing to their different molecular machineries and substrate preferences. However, elegant studies conducted in the last decade have demonstrated the interplay between autophagy and UPS at the molecular and functional levels. Among the most prominent molecule facilitating autophagy and UPS crosstalk is ubiquitin and recent studies have implicated the role of small Ub-like modifiers (SUMO) in autophagy as well. This chapter highlights the current understandings of the role of ubiquitin and SUMO in the regulation of autophagy read more ...
