Article
Mso1p regulates membrane fusion through interactions with the putative N-peptide-binding area in Sec1p domain 1.
Molecular biology of the cell - 15 Apr 2010
Weber Marion, Chernov Konstantin, Turakainen Hilkka, Wohlfahrt Gerd, Pajunen Maria, Savilahti Harri, Jäntti Jussi
Abstract excerpt
Sec1p/Munc18 (SM) family proteins regulate SNARE complex function in membrane fusion through their interactions with syntaxins. In addition to syntaxins, only a few SM protein interacting proteins are known and typically, their binding modes with SM proteins are poorly characterized. We previously identified Mso1p as a Sec1p-binding protein and showed that it is involved in membrane fusion regulation. Here we...
Topics
- Amino Acid Substitution
- Binding Sites
- Membrane Fusion
- Membrane Proteins
- Models, Molecular
- Munc18 Proteins
- Mutation
- Peptides
- Protein Binding
- Protein Interaction Mapping