Fusion of the endoplasmic reticulum by membrane-bound GTPases.
The endoplasmic reticulum (ER) membrane forms an elaborate network of tubules and sheets that is continuously remodeled. This dynamic behavior requires membrane fusion that is mediated by dynamin-like GTPases: the atlastins in metazoans and Sey1p and related proteins in yeast and plants. Crystal structures of the cytosolic domains of these membrane proteins and biochemical experiments can now be integrated into a model that explains many aspects of the molecular mechanism by which these membrane-bound GTPases mediate membrane fusion.
National Laboratory of Biomacromolecules, Institute of Biophysics, Chinese Academy of Sciences, Beijing 100101, China. Electronic address: huj@ibp.ac.cn.
Junjie
J
Hu
Howard Hughes Medical Institute and Department of Cell Biology, Harvard Medical School, Boston, MA 02115, United States. Electronic address: tom_rapoport@hms.harvard.edu.
Tom A
TA
Rapoport
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D020558:GTP Phosphohydrolases / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008561:Membrane Fusion; D008958:Models, Molecular; D050600:SNARE Proteins / Q000378:metabolism
D050600:SNARE Proteins; D020558:GTP Phosphohydrolases
Atlastin; Endoplasmic reticulum; Membrane fusion