The atlastin membrane anchor forms an intramembrane hairpin that does not span the phospholipid bilayer.

ABSTRACT: The endoplasmic reticulum (ER) is composed of flattened sheets and interconnected tubules that extend throughout the cytosol and makes physical contact with all other cytoplasmic organelles. This cytoplasmic distribution requires continuous remodeling. These discrete ER morphologies require specialized proteins that drive and maintain membrane curvature. The GTPase atlastin is required for homotypic fusion of ER tubules. All atlastin homologs possess a conserved domain architecture consisting of a GTPase domain, a three-helix bundle middle domain, a hydrophobic membrane anchor, and a C-terminal cytosolic tail. Here, we examined several Drosophila-human atlastin chimeras to identify functional domains of human atlastin-1 in vitro Although all chimeras could hydrolyze GTP, only

SUBMITTER: Betancourt-Solis MA 

PROVIDER: S-EPMC6290144 | biostudies-literature | 2018 Nov

REPOSITORIES: biostudies-literature