A cascade of multiple proteins and lipids catalyzes membrane fusion

Recent studies suggest revisions to the SNARE paradigm of membrane fusion. Membrane tethers and/or SNAREs recruit proteins of the Sec 1/Munc18 family to catalyze SNARE assembly into -complexes. SNARE-domain zippering draws the bilayers into immediate apposition and provides a platform to position fu...

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Veröffentlicht in:	Molecular biology of the cell 2017-03, Vol.28 (6), p.707-711
Hauptverfasser:	Wickner, William, Rizo, Josep
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Humans Lipids Membrane Fusion - physiology Membrane Proteins - metabolism Munc18 Proteins - metabolism Munc18 Proteins - physiology Protein Binding SNARE Proteins - metabolism SNARE Proteins - physiology Soluble N-Ethylmaleimide-Sensitive Factor Attachment Proteins
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Beschreibung
Zusammenfassung:	Recent studies suggest revisions to the SNARE paradigm of membrane fusion. Membrane tethers and/or SNAREs recruit proteins of the Sec 1/Munc18 family to catalyze SNARE assembly into -complexes. SNARE-domain zippering draws the bilayers into immediate apposition and provides a platform to position fusion triggers such as Sec 17/α-SNAP and/or synaptotagmin, which insert their apolar "wedge" domains into the bilayers, initiating the lipid rearrangements of fusion.
ISSN:	1059-1524 1939-4586
DOI:	10.1091/mbc.e16-07-0517