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Volume 272, Number 50, Issue of December 12, 1997 pp. 31459-31464
(Received for publication, September 16, 1997, and in revised form, October 8, 1997)
From the Howard Hughes Medical Institute and the Department of
Molecular Genetics, University of Texas Southwestern Medical
School, Dallas, Texas 75235
Munc18-1 is a neuronal protein that interacts
with syntaxin 1 and is required for synaptic vesicle exocytosis. We
have now identified two Munc18-1-interacting proteins called Mint1 and Mint2 that may mediate the function of Munc18-1. Mint proteins are
detectable only in brain and are composed of an N-terminal sequence
that binds Munc18-1, a middle phosphotyrosine-binding domain, and two
C-terminal PDZ domains thought to attach proteins to the plasma
membrane. In brain, Mint proteins are part of a multimeric complex
containing Munc18-1 and syntaxin that likely functions as an
intermediate in synaptic vesicle docking/fusion. The
phosphotyrosine-binding domain specifically binds to
phosphatidylinositol phosphates known to be produced during vesicle
exocytosis (Hay, J. C., Fisette, P. L., Jenkins, G. H.,
Fukami, K., Takonawa, T., Anderson, R. A., and Martin, T. F. J. (1995) Nature 374, 173-177). Our data suggest a
model whereby local production of phosphatidylinositol phosphates may
trigger the binding of vesicles to the active zone via the
Mint·Munc18-1 complex in conjunction with syntaxin 1.
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