title: How can proteolipids be central players in membrane fusion?
abstract: Proton transport ATPases have been celebrated as rotating motors that energize membranes. Now studies of membrane fusion in yeast suggest that the hydrophobic subunits of the vacuolar ATPase participate in formation of fusion pores. This work confirms previous studies showing that membrane approximation by alpha-helical protein bundles is inadequate for complete intracellular fusion and reopens a debate over whether the core of the central intermediate of membrane fusion is lipidic or proteinaceous.
authors.affiliation: Laboratory of Cellular and Molecular Biophysics, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892-1855, USA. joshz@helix.nih.gov
authors.forename: J
authors.initials: J
authors.lastname: Zimmerberg
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000378:metabolism; D006801:Humans; D007425:Intracellular Membranes / Q000502:physiology; D008561:Membrane Fusion / Q000502:physiology*; D008563:Membrane Lipids / Q000502:physiology*; D008565:Membrane Proteins / Q000378:metabolism; D008958:Models, Molecular; D011510:Proteolipids / Q000502:physiology*; D015398:Signal Transduction
chemical_list: D008563:Membrane Lipids; D008565:Membrane Proteins; D011510:Proteolipids; D000251:Adenosine Triphosphatases; D002118:Calcium