{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Popelka H"],"funding":["University of Michigan","National Institute of General Medical Sciences","NIGMS NIH HHS"],"pagination":["166809"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7924733"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["433(5)"],"pubmed_abstract":["Macroautophagy is a bulk degradation mechanism in eukaryotic cells. Efficiency of an essential step of this process in yeast, Atg8 lipidation, relies on the presence of Atg16, a subunit of the Atg12-Atg5-Atg16 complex acting as the E3-like enzyme in the ubiquitination-like reaction. A current view on the functional structure of Atg16 in the yeast S. cerevisiae comes from the two crystal structures that reveal the Atg5-interacting α-helix linked via a flexible linker to another α-helix of Atg16, which then assembles into a homodimer. This view does not explain the results of previous in vitro studies revealing Atg16-dependent deformations of membranes and liposome-binding of the Atg12-Atg5 conjugate upon addition of Atg16. Here we show that Atg16 acts as both a homodimerizing and peripheral"],"journal":["Journal of molecular biology"],"pubmed_title":["Membrane Binding and Homodimerization of Atg16 Via Two Distinct Protein Regions is Essential for Autophagy in Yeast."],"pmcid":["PMC7924733"],"funding_grant_id":["GM113132","GM128663","P20 GM113132","R35 GM128663","R35 GM131919","GM131919"],"pubmed_authors":["Metur SP","Leary KA","Ragusa MJ","Reinhart EF","Popelka H","Klionsky DJ"],"additional_accession":[]},"is_claimable":false,"name":"Membrane Binding and Homodimerization of Atg16 Via Two Distinct Protein Regions is Essential for Autophagy in Yeast.","description":"Macroautophagy is a bulk degradation mechanism in eukaryotic cells. Efficiency of an essential step of this process in yeast, Atg8 lipidation, relies on the presence of Atg16, a subunit of the Atg12-Atg5-Atg16 complex acting as the E3-like enzyme in the ubiquitination-like reaction. A current view on the functional structure of Atg16 in the yeast S. cerevisiae comes from the two crystal structures that reveal the Atg5-interacting α-helix linked via a flexible linker to another α-helix of Atg16, which then assembles into a homodimer. This view does not explain the results of previous in vitro studies revealing Atg16-dependent deformations of membranes and liposome-binding of the Atg12-Atg5 conjugate upon addition of Atg16. Here we show that Atg16 acts as both a homodimerizing and peripheral","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Mar","modification":"2026-05-31T07:11:31.534Z","creation":"2025-04-04T07:57:00.135Z"},"accession":"S-EPMC7924733","cross_references":{"pubmed":["33484718"],"doi":["10.1016/j.jmb.2021.166809"]}}