Characterization of two distinct binding modes between syntaxin 4 and Munc18c

被引：19

作者：

Aran, Veronica ^{[1
]}

Brandie, Fiona M. ^{[1
]}

Boyd, Alasdair R. ^{[1
]}

Kantidakis, Theodoros ^{[1
]}

Rideout, Elizabeth J. ^{[1
]}

Kelly, Sharon M. ^{[1
]}

Gould, Gwyn W. ^{[1
]}

Bryant, Nia J. ^{[1
]}

机构：

[1] Univ Glasgow, Fac Biomed & Life Sci, Div Mol & Cellular Biol, Henry Wellcome Lab Cell Biol, Glasgow G12 8QQ, Lanark, Scotland

来源：

BIOCHEMICAL JOURNAL | 2009年 / 419卷

基金：

英国生物技术与生命科学研究理事会;

关键词：

membrane fusion; Munc18c; Sec1/Munc18 protein (SM protein); soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor (SNARE); syntaxin; 4; vacuolar protein sorting 45 (Vps45p); SEC1/MUNC18; PROTEINS; VESICLE TRAFFICKING; MEMBRANE-FUSION; COMPLEX; EXOCYTOSIS; SNARES; GLUT4; GOLGI;

D O I：

10.1042/BJ20082293

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Interaction of SM (Sec1/Munc18) proteins with their cognate syntaxins represents an important regulatory mechanism of SNARE (soluble N-ethylmaleimide-sensitive fusion protein-attachment protein receptor)-mediated membrane fusion. Understanding the conserved mechanisms 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. In the present study, we have identified a hitherto uncharacterized mode of binding between syntaxin 4 and Munc18c that is independent of the binding mode shown previously to utilize the N-terminal peptide of syntaxin 4. Our data demonstrate that syntaxin 4 and Munc18c interact via two distinct modes of binding, analogous to those employed by syntaxin 1a-Munc18a and syntaxin 16-Vps45p (vacuolar protein sorting 45). 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.

引用

页码：655 / 660

页数：6

共 23 条

[1] Structural basis for the Golgi membrane recruitment of Sly1p by Sed5p [J].