Results 21 to 30 of about 18,950 (216)
Mammalian Atg8s: One is simply not enough [PDF]
Autophagy, 2010 Yeast Atg8, a key factor in the autophagic process, is a ubiquitin-like protein that undergoes a unique conjugation to phosphatidylethanolamine (PE). Atg8 plays a dual role in early stages of autophagosome formation: It was implicated in recruitment of cargo proteins such as Atg19 and Atg32 for Cvt and mitophagy, respectively, and in autophagosome ...
Hilla, Weidberg +3 more
openaire +2 more sources
Toward effective Atg8‐based ATTECs: Approaches and perspectives
Journal of Cellular Biochemistry, 2023 AbstractInduction of Atg8‐family protein (LC3/GABARAP proteins in human) interactions with target proteins of interest by proximity‐inducing small molecules offers the possibility for novel targeted protein degradation approaches. However, despite intensive screening campaigns during the last 5 years, no potent ligands for LC3/GABARAPs have been ...
Martin P. Schwalm +2 more
openaire +3 more sources
Activation and targeting of ATG8 protein lipidation [PDF]
Cell Discovery, 2020 AbstractATG8 family proteins are evolutionary conserved ubiquitin-like modifiers, which become attached to the headgroup of the membrane lipid phosphatidylethanolamine in a process referred to as lipidation. This reaction is carried out analogous to the conjugation of ubiquitin to its target proteins, involving the E1-like ATG7, the E2-like ATG3 and ...
Martens, Sascha, Fracchiolla, Dorotea
openaire +4 more sources
Lipidation status of single membrane-associated ATG8 proteins
Trends in Biochemical Sciences, 2021 ATG8 are core autophagy proteins, the lipidated forms of which decorate double-membraned autophagosomes, as well as single-membraned organelles such as endolysosomes. Recent studies from the Florey and Münz laboratories delineate the status of single membrane-associated ATG8 proteins by indicating that their membrane anchoring can involve ...
Viret, Christophe, Faure, Mathias
openaire +6 more sources
Atg8 Controls Phagophore Expansion during Autophagosome Formation [PDF]
Molecular Biology of the Cell, 2008 Autophagy is a potent intracellular degradation process with pivotal roles in health and disease. Atg8, a lipid-conjugated ubiquitin-like protein, is required for the formation of autophagosomes, double-membrane vesicles responsible for the delivery of cytoplasmic material to lysosomes.
Zhiping, Xie +2 more
openaire +2 more sources
Autophagy Reports, 2023 There are two types of autophagy, non-selective (bulk) autophagy, in which substrates are randomly incorporated into autophagosomes, and selective autophagy, in which substrates are specifically targeted.
Takashi Kikuma, Joichiro Nishio
doaj +1 more source
Structural biology of the Atg8 and Atg12 conjugation systems
Autophagy Reports, 2023 Atg8 and Atg12 are ubiquitin-like proteins, conjugated to phosphatidylethanolamine (PE) and Atg5, respectively, through enzymatic reactions similar to ubiquitylation.
Nobuo N. Noda
doaj +1 more source
The EMBO Journal, 2015 Autophagosome biogenesis requires two ubiquitin-like conjugation systems. One couples ubiquitin-like Atg8 to phosphatidylethanolamine, and the other couples ubiquitin-like Atg12 to Atg5. Atg12~Atg5 then forms a heterodimer with Atg16. Membrane recruitment of the Atg12~Atg5/Atg16 complex defines the Atg8 lipidation site.
Juris, Lisa +5 more
openaire +3 more sources
Distribution, cleavage and lipidation of Atg8 fusion proteins in Spodoptera litura Sl-HP cells.
PLoS ONE, 2014 Atg8 proteins fused with tags are commonly used to detect autophagy. The expression patterns of Lepidopteran insect Atg8 are relatively well documented. However, the influence of protein tags on characterization of Atg8 is still not very clear.
Xiaojuan Zhang +8 more
doaj +1 more source
Plant Signaling & Behavior, 2023 Potato virus Y (PVY) is an aphid-transmitted potyvirus that affects economically important solanaceous species. In this study, the phenomena and mechanisms following infection with PVY were investigated in tobacco (Nicotiana benthamiana).
Won-Jin Kim +4 more
doaj +1 more source