title: Membrane traffic: controlling membrane fusion by modifying NSF.
abstract: Recent studies show that NSF, isolated over 15 years ago as a protein required for membrane fusion in vitro, can be reversibly inactivated by both S-nitrosylation and tyrosine phosphorylation. Different cell types use distinct post-translational modifications of NSF for localized regulation of membrane fusion.
authors.affiliation: The Physiological Laboratory, School of Biomedical Sciences, University of Liverpool, Crown St., P.O. Box 147, Liverpool L69 3BX, UK. amorgan@liv.ac.uk
authors.forename: Alan
authors.initials: A
authors.lastname: Morgan
authors.forename: Robert D
authors.initials: RD
authors.lastname: Burgoyne
mesh_terms: D008561:Membrane Fusion / Q000502:physiology*; D052066:N-Ethylmaleimide-Sensitive Proteins; D010766:Phosphorylation; D011499:Protein Processing, Post-Translational / Q000502:physiology*; D017434:Protein Structure, Tertiary; D050600:SNARE Proteins; D033921:Vesicular Transport Proteins / Q000378:metabolism* / Q000502:physiology
chemical_list: D050600:SNARE Proteins; D033921:Vesicular Transport Proteins; D052066:N-Ethylmaleimide-Sensitive Proteins