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.
|Number of pages||10|
|State||Published - May 22 2007|
Bibliographical noteFunding Information:
We apologize to the excellent, but alas uncited, researchers who have contributed to our understanding of NSF. Due to space constraints we could not discuss all of the published studies of NSF function. The authors thank the Whiteheart laboratory for their care in reading this manuscript. We specifically thank Dr. Elena A. Matveeva whose efforts have made much of the work discussed possible. We are indebted to Dr. Phyllis Hanson (Washington University) for her insightful comments over the years and to Dr. Elizabeth Kubalek-Wilson (Scripps Research Institute) for her perseverance in our studies of NSF’s structure. This work is supported by Grants from the National Institutes of Health, NS046242 (to S.W.W.) and from the Department of Veterans Affairs (to J.T.S.).
- Post-translational modification
ASJC Scopus subject areas
- Structural Biology
- Molecular Biology
- Cell Biology