The interaction of Munc18-1 helix 11 and 12 with the central region of the VAMP2 SNARE motif is essential for SNARE templating and synaptic transmission
Sec1/Munc18 proteins play a key role in initiating the assembly of N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes, the molecular fusion machinery. Employing comparative structure modeling, site specific crosslinking by single amino acid substitutions with the photoac...
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| Hauptverfasser: | , , , , , , , , , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
14 October 2020
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| In: |
eNeuro
Year: 2020, Jahrgang: 7, Heft: 6 |
| ISSN: | 2373-2822 |
| DOI: | 10.1523/ENEURO.0278-20.2020 |
| Online-Zugang: | Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1523/ENEURO.0278-20.2020
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| Verfasserangaben: | Timon André, Jessica Classen, Philipp Brenner, Matthew J Betts, Bernhard Dörr, Susanne Kreye, Birte Zuidinga, Marieke Meijer, Robert B Russell, Matthijs Verhage, and Thomas H Söllner |
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| 245 | 1 | 4 | |a The interaction of Munc18-1 helix 11 and 12 with the central region of the VAMP2 SNARE motif is essential for SNARE templating and synaptic transmission |c Timon André, Jessica Classen, Philipp Brenner, Matthew J Betts, Bernhard Dörr, Susanne Kreye, Birte Zuidinga, Marieke Meijer, Robert B Russell, Matthijs Verhage, and Thomas H Söllner |
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| 520 | |a Sec1/Munc18 proteins play a key role in initiating the assembly of N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complexes, the molecular fusion machinery. Employing comparative structure modeling, site specific crosslinking by single amino acid substitutions with the photoactivatable unnatural amino acid p-Benzoyl-phenylalanine (Bpa) and reconstituted vesicle docking/fusion assays, we mapped the binding interface between Munc18-1 and the neuronal v-SNARE VAMP2 with single amino acid resolution. Our results show that helices 11 and 12 of domain 3a in Munc18-1 interact with the VAMP2 SNARE motif covering the region from layers À4 to 15. Residue Q301 in helix 11 plays a pivotal role in VAMP2 binding and template complex formation. A VAMP2 binding deficient mutant, Munc18-1 Q301D, does not stimulate lipid mixing in a reconstituted fusion assay. The neuronal SNARE-organizer Munc13-1, which also binds VAMP2, does not bypass the requirement for the Munc18-1·VAMP2 interaction. Importantly, Munc18-1 Q301D expression in Munc18-1 deficient neurons severely reduces synaptic transmission, demonstrating the physiological significance of the Munc18-1·VAMP2 interaction. | ||
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