Cellular functions of NSF: not just SNAPs and SNAREs.
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 beta2-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.
Zhao
Chunxia
C
Department of Molecular and Cellular Biochemistry, University of Kentucky College of Medicine, 741 South Limestone, BBSRB B261, Lexington, KY 40536, USA.
Slevin
John T
JT
Whiteheart
Sidney W
SW
D000818:Animals; D003599:Cytoskeleton / Q000378:metabolism; D008958:Models, Molecular; D052066:N-Ethylmaleimide-Sensitive Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D050600:SNARE Proteins / Q000378:metabolism*; D052067:Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins / Q000378:metabolism*; D022161:Transport Vesicles / Q000378:metabolism
D050600:SNARE Proteins; D052067:Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins; D052066:N-Ethylmaleimide-Sensitive Proteins