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Cellular functions of NSF: Not just SNAPs and SNAREs
Author(s) -
Zhao Chunxia,
Slevin John T.,
Whiteheart Sidney W.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.03.032
Subject(s) - snare complex , microbiology and biotechnology , chaperone (clinical) , atp hydrolysis , phosphorylation , intracellular , lipid bilayer fusion , chemistry , protein subunit , atpase , transport protein , biology , biochemistry , membrane , medicine , pathology , gene , enzyme
N ‐ethylmaleimide sensitive factor (NSF) is an ATPases associated with various cellular activities protein (AAA), broadly required for intracellular membrane fusion. NSF functions as a SNAP receptor (SNARE) chaperone which binds, through soluble NSF attachment proteins (SNAPs), to SNARE complexes and utilizes the energy of ATP hydrolysis to disassemble them thus facilitating SNARE recycling. While this is a major function of NSF, it does seem to interact with other proteins, such as the AMPA receptor subunit, GluR2, and β2‐AR and is thought to affect their trafficking patterns. New data suggest that NSF may be regulated by transient post‐translational modifications such as phosphorylation and nitrosylation. These new aspects of NSF function as well as its role in SNARE complex dynamics will be discussed.