Characterisation of two distinct binding modes between Syntaxin 4 and Munc18c.
Résumé
Interaction of Sec1/Munc18 (SM) proteins with their cognate syntaxins represents an important regulatory mechanism of SNARE-mediated membrane fusion. Understanding the conserved mechanism by which SM proteins function in this process has proved challenging, largely due to an apparent lack of conservation of binding mechanisms between different SM/syntaxin pairs. Here we have identified a hitherto uncharacterised mode of binding between syntaxin 4 and Munc18c that is independent of the binding mode previously shown to utilise the N-terminal peptide of syntaxin 4. Our data demonstrate that syntaxin 4/Munc18c interact via two distinct modes of binding, analogous to those employed by syntaxin 1a/Munc18a and syntaxin 16/Vps45. These data support the notion that all syntaxin/SM proteins bind using conserved mechanisms, and pave the way for the formulation of unifying hypotheses of SM protein function.
Origine : Fichiers produits par l'(les) auteur(s)
Loading...