title: Structures of Atg7-Atg3 and Atg7-Atg10 reveal noncanonical mechanisms of E2 recruitment by the autophagy E1.
abstract: Central to most forms of autophagy are two ubiquitin-like proteins (UBLs), Atg8 and Atg12, which play important roles in autophagosome biogenesis, substrate recruitment to autophagosomes, and other aspects of autophagy. Typically, UBLs are activated by an E1 enzyme that (1) catalyzes adenylation of the UBL C terminus, (2) transiently covalently captures the UBL through a reactive thioester bond between the E1 active site cysteine and the UBL C terminus, and (3) promotes transfer of the UBL C terminus to the catalytic cysteine of an E2 conjugating enzyme. The E2, and often an E3 ligase enzyme, catalyzes attachment of the UBL C terminus to a primary amine group on a substrate. Here, we summarize our recent work reporting the structural and mechanistic basis for E1-E2 protein interactions in autophagy.
authors: Department of Structural Biology, St. Jude Children's Research Hospital, Memphis, TN, USA.
authors: Stephen E
authors: SE
authors: Kaiser
authors: Yu
authors: Y
authors: Qiu
authors: Julie E
authors: JE
authors: Coats
authors: Kai
authors: K
authors: Mao
authors: Daniel J
authors: DJ
authors: Klionsky
authors: Brenda A
authors: BA
authors: Schulman
mesh_terms: D001343:Autophagy; D008954:Models, Biological; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000166:cytology* / Q000201:enzymology*; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism*; D044764:Ubiquitin-Activating Enzymes / Q000378:metabolism*; D044763:Ubiquitin-Conjugating Enzymes / Q000378:metabolism*; D014452:Ubiquitins / Q000378:metabolism
chemical_list: D029701:Saccharomyces cerevisiae Proteins; D014452:Ubiquitins; D044763:Ubiquitin-Conjugating Enzymes; D044764:Ubiquitin-Activating Enzymes
keywords: Atg10; Atg12; Atg3; Atg7; Atg8; E1 enzyme; E2 enzyme; ubiquitin-like protein