Activation and targeting of ATG8 protein lipidation

Sascha Martens; Dorotea Fracchiolla

doi:10.1038/s41421-020-0155-1

Titel

Activation and targeting of ATG8 protein lipidation

Autor*in

Department für Biochemie und Zellbiologie (bis 2023-12-31), Zentrum für Molekulare Biologie (bis 2023-12-31), Universität Wien

Dorotea Fracchiolla

Department für Biochemie und Zellbiologie (bis 2023-12-31), Zentrum für Molekulare Biologie (bis 2023-12-31), Universität Wien

Abstract

ATG8 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 the E3-like ATG12–ATG5–ATG16 complex, which determines the site of lipidation. ATG8 lipidation is a hallmark of autophagy where these proteins are involved in autophagosome formation, the fusion of autophagosomes with lysosomes and cargo selection. However, it has become evident that ATG8 lipidation also occurs in processes that are not directly related to autophagy. Here we discuss recent insights into the targeting of ATG8 lipidation in autophagy and other pathways with special emphasis on the recruitment and activation of the E3-like complex.

Stichwort

MacroautophagyPhagocytosis

Objekt-Typ

journal article

Sprache

Englisch [eng]

Persistent identifier

phaidra.univie.ac.at/o:1415681

DOI

10.1038/s41421-020-0155-1

Erschienen in

Titel