TY  - JOUR
A1  - Gubas, Andrea
A1  - Đikić, Ivan
T1  - A guide to the regulation of selective autophagy receptors
T2  - The FEBS journal
N2  - Autophagy is a highly conserved catabolic process cells use to maintain their homeostasis by degrading misfolded, damaged and excessive proteins, nonfunctional organelles, foreign pathogens and other cellular components. Hence, autophagy can be nonselective, where bulky portions of the cytoplasm are degraded upon stress, or a highly selective process, where preselected cellular components are degraded. To distinguish between different cellular components, autophagy employs selective autophagy receptors, which will link the cargo to the autophagy machinery, thereby sequestering it in the autophagosome for its subsequent degradation in the lysosome. Autophagy receptors undergo post-translational and structural modifications to fulfil their role in autophagy, or upon executing their role, for their own degradation. We highlight the four most prominent protein modifications – phosphorylation, ubiquitination, acetylation and oligomerisation – that are essential for autophagy receptor recruitment, function and turnover. Understanding the regulation of selective autophagy receptors will provide deeper insights into the pathway and open up potential therapeutic avenues.
KW  - autophagy
KW  - oligomerisation
KW  - phosphorylation
KW  - receptor
KW  - ubiquitination
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/63884
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-638843
SN  - 1742-4658
N1  - Early View: Online Version before inclusion in an issue
N1  - Our research is supported by the Deutsche Forschungsgemeinschaft (DFG, German Research Foundation) – Project Number 259130777 – SFB 1177, the grants from Else Kroener Fresenius Stiftung and Dr. Rolf M. Schwiete Stiftung.
N1  - Version of Record: http://nbn-resolving.de/urn/resolver.pl?urn:nbn:de:hebis:30:3-638632
IS  - online version before inclusion in an issue
SP  - 1
EP  - 15
PB  - Wiley-Blackwell
CY  - Oxford [u.a.]
ER  -