Cellular functions of NSF: Not just SNAPs and SNAREs

Chunxia Zhao; John T. Slevin; Sidney W. Whiteheart

doi:10.1016/j.febslet.2007.03.032

Cellular functions of NSF: Not just SNAPs and SNAREs

Chunxia Zhao, John T. Slevin, Sidney W. Whiteheart

Research output: Contribution to journal › Short survey › peer-review

106 Scopus citations

Abstract

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.

Original language	English
Pages (from-to)	2140-2149
Number of pages	10
Journal	FEBS Letters
Volume	581
Issue number	11
DOIs	https://doi.org/10.1016/j.febslet.2007.03.032
State	Published - May 22 2007

Bibliographical note

Funding 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.).

Keywords

GluR2
NSF
Post-translational modification
SNARE
α-SNAP
β2-AR

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

Access to Document

10.1016/j.febslet.2007.03.032

Cite this

@article{51e728f01aa64647974189bb918c5f96,

title = "Cellular functions of NSF: Not just SNAPs and SNAREs",

abstract = "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.",

keywords = "GluR2, NSF, Post-translational modification, SNARE, α-SNAP, β2-AR",

author = "Chunxia Zhao and Slevin, {John T.} and Whiteheart, {Sidney W.}",

note = "Funding 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{\textquoteright}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.).",

year = "2007",

month = may,

day = "22",

doi = "10.1016/j.febslet.2007.03.032",

language = "English",

volume = "581",

pages = "2140--2149",

number = "11",

}

TY - JOUR

T1 - Cellular functions of NSF

T2 - Not just SNAPs and SNAREs

AU - Zhao, Chunxia

AU - Slevin, John T.

AU - Whiteheart, Sidney W.

N1 - Funding 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.).

PY - 2007/5/22

Y1 - 2007/5/22

N2 - 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.

AB - 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.

KW - GluR2

KW - NSF

KW - Post-translational modification

KW - SNARE

KW - α-SNAP

KW - β2-AR

UR - http://www.scopus.com/inward/record.url?scp=34248227248&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34248227248&partnerID=8YFLogxK

U2 - 10.1016/j.febslet.2007.03.032

DO - 10.1016/j.febslet.2007.03.032

M3 - Short survey

C2 - 17397838

AN - SCOPUS:34248227248

SN - 0014-5793

VL - 581

SP - 2140

EP - 2149

JO - FEBS Letters

JF - FEBS Letters

IS - 11

ER -

Cellular functions of NSF: Not just SNAPs and SNAREs

Abstract

Bibliographical note

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this