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.
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Research Article|
April 14 2009
Characterization of two distinct binding modes between syntaxin 4 and Munc18c
Veronica Aran;
Veronica Aran
1Henry Wellcome Laboratory of Cell Biology, Division of Molecular and Cellular Biology, Davidson Building, Faculty of Biomedical and Life Science, University of Glasgow, Glasgow G12 8QQ, U.K.
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Fiona M. Brandie;
Fiona M. Brandie
1Henry Wellcome Laboratory of Cell Biology, Division of Molecular and Cellular Biology, Davidson Building, Faculty of Biomedical and Life Science, University of Glasgow, Glasgow G12 8QQ, U.K.
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Alasdair R. Boyd;
Alasdair R. Boyd
1Henry Wellcome Laboratory of Cell Biology, Division of Molecular and Cellular Biology, Davidson Building, Faculty of Biomedical and Life Science, University of Glasgow, Glasgow G12 8QQ, U.K.
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Theodoros Kantidakis;
Theodoros Kantidakis
1Henry Wellcome Laboratory of Cell Biology, Division of Molecular and Cellular Biology, Davidson Building, Faculty of Biomedical and Life Science, University of Glasgow, Glasgow G12 8QQ, U.K.
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Elizabeth J. Rideout;
Elizabeth J. Rideout
1Henry Wellcome Laboratory of Cell Biology, Division of Molecular and Cellular Biology, Davidson Building, Faculty of Biomedical and Life Science, University of Glasgow, Glasgow G12 8QQ, U.K.
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Sharon M. Kelly;
Sharon M. Kelly
1Henry Wellcome Laboratory of Cell Biology, Division of Molecular and Cellular Biology, Davidson Building, Faculty of Biomedical and Life Science, University of Glasgow, Glasgow G12 8QQ, U.K.
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Gwyn W. Gould;
Gwyn W. Gould
1Henry Wellcome Laboratory of Cell Biology, Division of Molecular and Cellular Biology, Davidson Building, Faculty of Biomedical and Life Science, University of Glasgow, Glasgow G12 8QQ, U.K.
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Nia J. Bryant
Nia J. Bryant
1
1Henry Wellcome Laboratory of Cell Biology, Division of Molecular and Cellular Biology, Davidson Building, Faculty of Biomedical and Life Science, University of Glasgow, Glasgow G12 8QQ, U.K.
1To whom correspondence should be addressed (email [email protected]).
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Publisher: Portland Press Ltd
Received:
November 26 2008
Revision Received:
January 07 2009
Accepted:
February 04 2009
Accepted Manuscript online:
February 04 2009
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2009 Biochemical Society
2009
Biochem J (2009) 419 (3): 655–660.
Article history
Received:
November 26 2008
Revision Received:
January 07 2009
Accepted:
February 04 2009
Accepted Manuscript online:
February 04 2009
Citation
Veronica Aran, Fiona M. Brandie, Alasdair R. Boyd, Theodoros Kantidakis, Elizabeth J. Rideout, Sharon M. Kelly, Gwyn W. Gould, Nia J. Bryant; Characterization of two distinct binding modes between syntaxin 4 and Munc18c. Biochem J 1 May 2009; 419 (3): 655–660. doi: https://doi.org/10.1042/BJ20082293
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