title: GTP-dependent membrane fusion.
abstract: Shape changes and topological remodeling of membranes are essential for the identity of organelles and membrane trafficking. Although all cellular membranes have common features, membranes of different organelles create unique environments that support specialized biological functions. The endoplasmic reticulum (ER) is a prime example of this specialization, as its lipid bilayer forms an interconnected system of cisternae, vesicles, and tubules, providing a highly compartmentalized structure for a multitude of biochemical processes. A variety of peripheral and integral membrane proteins that facilitate membrane curvature generation, fission, and/or fusion have been identified over the past two decades. Among these, the dynamin-related proteins (DRPs) have emerged as key players. Here, we review recent advances in our functional and molecular understanding of fusion DRPs, exemplified by atlastin, an ER-resident DRP that controls ER structure, function, and signaling.
authors.affiliation: Department of Biochemistry and Cell Biology, Rice University, Houston, Texas 77005; email: mcnew@rice.edu.
authors.forename: James A
authors.initials: JA
authors.lastname: McNew
authors.forename: Holger
authors.initials: H
authors.lastname: Sondermann
authors.forename: Tina
authors.initials: T
authors.lastname: Lee
authors.forename: Mike
authors.initials: M
authors.lastname: Stern
authors.forename: Federica
authors.initials: F
authors.lastname: Brandizzi
mesh_terms: D000818:Animals; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism*; D006801:Humans; D008561:Membrane Fusion; D008565:Membrane Proteins / Q000378:metabolism; D010944:Plants / Q000378:metabolism; D015003:Yeasts / Q000166:cytology / Q000378:metabolism
chemical_list: D008565:Membrane Proteins; D006160:Guanosine Triphosphate