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Synaptotagmin-1 binds to PIP(2)-containing membrane but not to SNAREs at physiological ionic strength.

Abstract：

:The Ca(2+) sensor synaptotagmin-1 is thought to trigger membrane fusion by binding to acidic membrane lipids and SNARE proteins. Previous work has shown that binding is mediated by electrostatic interactions that are sensitive to the ionic environment. However, the influence of divalent or polyvalent ions, at physiological concentrations, on synaptotagmin's binding to membranes or SNAREs has not been explored. Here we show that binding of rat synaptotagmin-1 to membranes containing phosphatidylinositol 4,5-bisphosphate (PIP2) is regulated by charge shielding caused by the presence of divalent cations. Surprisingly, polyvalent ions such as ATP and Mg(2+) completely abrogate synaptotagmin-1 binding to SNAREs regardless of the presence of Ca(2+). Altogether, our data indicate that at physiological ion concentrations Ca(2+)-dependent synaptotagmin-1 binding is confined to PIP2-containing membrane patches in the plasma membrane, suggesting that membrane interaction of synaptotagmin-1 rather than SNARE binding triggers exocytosis of vesicles.

journal_name

Nat Struct Mol Biol

journal_title

Nature structural & molecular biology

authors

Park Y,Seo JB,Fraind A,Pérez-Lara A,Yavuz H,Han K,Jung SR,Kattan I,Walla PJ,Choi M,Cafiso DS,Koh DS,Jahn R

doi

10.1038/nsmb.3097

subject

Has Abstract

pub_date

2015-10-01 00:00:00

pages

815-23

issue

10

eissn

1545-9993

issn

1545-9985

pii

nsmb.3097

journal_volume

22

pub_type

杂志文章

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