Activity-dependent interactions of NSF and SNAP at living synapses

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

As core components of the neurotransmitter release apparatus, SNAREs, NSF and SNAPs mediate fusion of neurotransmitter-filled synaptic vesicles within specialized regions of the presynaptic plasma membrane known as active zones (AZs). The present study combines genetic approaches in Drosophila with biochemical and live-imaging methods to provide new insights into the in vivo behavior and interactions of NSF and SNAP in neurotransmitter release. This work employs a temperature-sensitive (TS) paralytic NSF mutant, comatose, to show that disruption of NSF function results in activity-dependent redistribution of NSF and SNAP to periactive zone (PAZ) regions of the presynaptic plasma membrane and accumulation of protein complexes containing SNAREs, NSF and SNAP. Fluorescence Resonance Energy Transfer (FRET) and Fluorescence Recovery After Photobleaching (FRAP) studies in comatose revealed that NSF and SNAP exhibit activity-dependent binding to each other within living presynaptic terminals as well as distinctive interactions and mobilities. These observations extend current models describing the spatial organization of NSF, SNAP and SNARE proteins in synaptic vesicle trafficking.

Original languageEnglish (US)
Pages (from-to)19-27
Number of pages9
JournalMolecular and Cellular Neuroscience
Volume47
Issue number1
DOIs
StatePublished - May 1 2011

Fingerprint

SNARE Proteins
Synapses
Neurotransmitter Agents
Synaptic Vesicles
Coma
Cell Membrane
Fluorescence Recovery After Photobleaching
Fluorescence Resonance Energy Transfer
Presynaptic Terminals
Drosophila
Blood Proteins
Membrane Proteins
Temperature

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Cellular and Molecular Neuroscience
  • Cell Biology

Cite this

@article{074a080d010544c285bac4a9a83831bf,
title = "Activity-dependent interactions of NSF and SNAP at living synapses",
abstract = "As core components of the neurotransmitter release apparatus, SNAREs, NSF and SNAPs mediate fusion of neurotransmitter-filled synaptic vesicles within specialized regions of the presynaptic plasma membrane known as active zones (AZs). The present study combines genetic approaches in Drosophila with biochemical and live-imaging methods to provide new insights into the in vivo behavior and interactions of NSF and SNAP in neurotransmitter release. This work employs a temperature-sensitive (TS) paralytic NSF mutant, comatose, to show that disruption of NSF function results in activity-dependent redistribution of NSF and SNAP to periactive zone (PAZ) regions of the presynaptic plasma membrane and accumulation of protein complexes containing SNAREs, NSF and SNAP. Fluorescence Resonance Energy Transfer (FRET) and Fluorescence Recovery After Photobleaching (FRAP) studies in comatose revealed that NSF and SNAP exhibit activity-dependent binding to each other within living presynaptic terminals as well as distinctive interactions and mobilities. These observations extend current models describing the spatial organization of NSF, SNAP and SNARE proteins in synaptic vesicle trafficking.",
author = "Wenhua Yu and Fumiko Kawasaki and Ordway, {Richard W.}",
year = "2011",
month = "5",
day = "1",
doi = "10.1016/j.mcn.2011.02.002",
language = "English (US)",
volume = "47",
pages = "19--27",
journal = "Molecular and Cellular Neurosciences",
issn = "1044-7431",
publisher = "Academic Press Inc.",
number = "1",

}

Activity-dependent interactions of NSF and SNAP at living synapses. / Yu, Wenhua; Kawasaki, Fumiko; Ordway, Richard W.

In: Molecular and Cellular Neuroscience, Vol. 47, No. 1, 01.05.2011, p. 19-27.

Research output: Contribution to journalArticle

TY - JOUR

T1 - Activity-dependent interactions of NSF and SNAP at living synapses

AU - Yu, Wenhua

AU - Kawasaki, Fumiko

AU - Ordway, Richard W.

PY - 2011/5/1

Y1 - 2011/5/1

N2 - As core components of the neurotransmitter release apparatus, SNAREs, NSF and SNAPs mediate fusion of neurotransmitter-filled synaptic vesicles within specialized regions of the presynaptic plasma membrane known as active zones (AZs). The present study combines genetic approaches in Drosophila with biochemical and live-imaging methods to provide new insights into the in vivo behavior and interactions of NSF and SNAP in neurotransmitter release. This work employs a temperature-sensitive (TS) paralytic NSF mutant, comatose, to show that disruption of NSF function results in activity-dependent redistribution of NSF and SNAP to periactive zone (PAZ) regions of the presynaptic plasma membrane and accumulation of protein complexes containing SNAREs, NSF and SNAP. Fluorescence Resonance Energy Transfer (FRET) and Fluorescence Recovery After Photobleaching (FRAP) studies in comatose revealed that NSF and SNAP exhibit activity-dependent binding to each other within living presynaptic terminals as well as distinctive interactions and mobilities. These observations extend current models describing the spatial organization of NSF, SNAP and SNARE proteins in synaptic vesicle trafficking.

AB - As core components of the neurotransmitter release apparatus, SNAREs, NSF and SNAPs mediate fusion of neurotransmitter-filled synaptic vesicles within specialized regions of the presynaptic plasma membrane known as active zones (AZs). The present study combines genetic approaches in Drosophila with biochemical and live-imaging methods to provide new insights into the in vivo behavior and interactions of NSF and SNAP in neurotransmitter release. This work employs a temperature-sensitive (TS) paralytic NSF mutant, comatose, to show that disruption of NSF function results in activity-dependent redistribution of NSF and SNAP to periactive zone (PAZ) regions of the presynaptic plasma membrane and accumulation of protein complexes containing SNAREs, NSF and SNAP. Fluorescence Resonance Energy Transfer (FRET) and Fluorescence Recovery After Photobleaching (FRAP) studies in comatose revealed that NSF and SNAP exhibit activity-dependent binding to each other within living presynaptic terminals as well as distinctive interactions and mobilities. These observations extend current models describing the spatial organization of NSF, SNAP and SNARE proteins in synaptic vesicle trafficking.

UR - http://www.scopus.com/inward/record.url?scp=79955480131&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=79955480131&partnerID=8YFLogxK

U2 - 10.1016/j.mcn.2011.02.002

DO - 10.1016/j.mcn.2011.02.002

M3 - Article

C2 - 21316453

AN - SCOPUS:79955480131

VL - 47

SP - 19

EP - 27

JO - Molecular and Cellular Neurosciences

JF - Molecular and Cellular Neurosciences

SN - 1044-7431

IS - 1

ER -