Ontology highlight
ABSTRACT:
SUBMITTER: Pendin D
PROVIDER: S-EPMC3182751 | biostudies-literature | 2011 Sep
REPOSITORIES: biostudies-literature
Pendin Diana D Tosetto Jessica J Moss Tyler J TJ Andreazza Camilla C Moro Stefano S McNew James A JA Daga Andrea A
Proceedings of the National Academy of Sciences of the United States of America 20110919 39
The mechanisms governing atlastin-mediated membrane fusion are unknown. Here we demonstrate that a three-helix bundle (3HB) within the middle domain is required for oligomerization. Mutation of core hydrophobic residues within these helices inactivates atlastin function by preventing membrane tethering and the subsequent fusion. GTP binding induces a conformational change that reorients the GTPase domain relative to the 3HB to permit self-association, but the ability to hydrolyze GTP is required ...[more]