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SNAREpins are functionally resistant to disruption by NSF and alphaSNAP
T Weber1, F Parlati, J A McNew
1Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
The Journal of Cell Biology
|June 1, 2000
Summary
Soluble NSF attachment protein (SNAP) receptor (SNARE) proteins mediate membrane fusion. Newly formed SNAREpins resist NSF-mediated disruption, ensuring fusion proceeds locally despite cellular conditions favoring SNARE disassembly.
Area of Science:
- Cell biology
- Biochemistry
- Membrane trafficking
Background:
- SNARE proteins are essential for membrane fusion processes.
- The ATPase NSF disassembles cis-SNARE complexes to recycle SNARE proteins.
- The mechanism preventing NSF from disrupting fusion-mediating trans-SNARE complexes was unknown.
Purpose of the Study:
- To investigate the functional resistance of trans-SNARE complexes (SNAREpins) to NSF-mediated disassembly.
- To understand how localized membrane fusion is maintained.
Main Methods:
- Experimental studies on isolated SNARE proteins and lipid bilayers.
- Analysis of SNARE complex formation and NSF interaction.
Main Results:
- Isolated SNARE proteins can fuse lipid bilayers.
- Trans-SNARE complexes (SNAREpins) are formed during fusion.
- SNAREpins exhibit functional resistance to NSF activity upon their formation.
- This resistance allows fusion to occur locally.
Conclusions:
- SNAREpins are intrinsically resistant to NSF.
- This resistance is established at the moment of SNAREpin formation.
- This mechanism ensures efficient and localized membrane fusion in cells.