Premium
Rebellious autophagy proteins bypass ATG8 lipidation, taking their own path to autophagic degradation
Author(s) -
Nguyen Thanh Ngoc,
Lazarou Michael
Publication year - 2020
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.15252/embj.2020106990
Subject(s) - autophagy , biology , lipid anchored protein , atg8 , microbiology and biotechnology , degradation (telecommunications) , protein degradation , path (computing) , biochemistry , apoptosis , engineering , telecommunications , computer science , programming language
LC3/GABARAP (hereafter ATG8) conjugation machineries have long been thought to play an essential role in autophagy by driving ATG8 lipidation on autophagosomal membranes. In this issue, Ohnstad et al (2020) describe an ATG8 lipidation bypass pathway which governs autophagy‐dependent turnover of NBR1, highlighting that there is more than one road to autophagic degradation.