The Journal of biological chemistry, 2013-08, Vol.288 (34), p.24984-24991
2013
Details
- Autor(en) / Beteiligte
- Titel
- Disassembly of All SNARE Complexes by N-Ethylmaleimide-sensitive Factor (NSF) Is Initiated by a Conserved 1:1 Interaction between α-Soluble NSF Attachment Protein (SNAP) and SNARE Complex
- Ist Teil von
- The Journal of biological chemistry, 2013-08, Vol.288 (34), p.24984-24991
- Ort / Verlag
- United States: Elsevier Inc
- Erscheinungsjahr
- 2013
- Link zum Volltext
- Quelle
- Alma/SFX Local Collection
- Beschreibungen/Notizen
- Vesicle trafficking in eukaryotic cells is facilitated by SNARE-mediated membrane fusion. The ATPase NSF (N-ethylmaleimide-sensitive factor) and the adaptor protein α-SNAP (soluble NSF attachment protein) disassemble all SNARE complexes formed throughout different pathways, but the effect of SNARE sequence and domain variation on the poorly understood disassembly mechanism is unknown. By measuring SNARE-stimulated ATP hydrolysis rates, Michaelis-Menten constants for disassembly, and SNAP-SNARE binding constants for four different ternary SNARE complexes and one binary complex, we found a conserved mechanism, not influenced by N-terminal SNARE domains. α-SNAP and the ternary SNARE complex form a 1:1 complex as revealed by multiangle light scattering. We propose a model of NSF-mediated disassembly in which the reaction is initiated by a 1:1 interaction between α-SNAP and the ternary SNARE complex, followed by NSF binding. Subsequent additional α-SNAP binding events may occur as part of a processive disassembly mechanism. Background: NSF and α-SNAP disassemble all SNARE complexes. Results: The disassembly kinetics is conserved for different ternary and binary SNARE complexes. α-SNAP and the ternary SNARE complex form a 1:1 complex. Conclusion: NSF uses a conserved mechanism to disassemble all SNARE complexes, starting from a 1:1 SNAP-SNARE complex interaction. Significance: We illuminate a broad mechanism allowing NSF to support SNARE-mediated exocytosis.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 0021-9258eISSN: 1083-351XDOI: 10.1074/jbc.M113.489807Titel-ID: cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_3750193
- Format
- –
- Schlagworte
- Adenosine Triphosphate - chemistry, Adenosine Triphosphate - genetics, Adenosine Triphosphate - metabolism, Animals, ATPases, Biophysics, Biosensors, Circular Dichroism (CD), Cricetinae, Cricetulus, Enzyme Kinetics, Fluorescence, Membrane Biology, Membrane Fusion, Models, Chemical, Multiprotein Complexes - chemistry, Multiprotein Complexes - genetics, Multiprotein Complexes - metabolism, N-Ethylmaleimide-Sensitive Proteins - chemistry, N-Ethylmaleimide-Sensitive Proteins - genetics, N-Ethylmaleimide-Sensitive Proteins - metabolism, Protein Binding, Protein-Protein Interactions, Rats, SNARE Proteins, SNARE Proteins - chemistry, SNARE Proteins - genetics, SNARE Proteins - metabolism, Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins - chemistry, Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins - genetics, Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins - metabolism, Structural Biology