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J Biol Chem, Vol. 274, Issue 39, 27347-27350, September 24, 1999

COMMUNICATION
Transient, Phorbol Ester-induced DOC2-Munc13 Interactions in Vivo

Rory R. Duncan, Andrea Betz, Michael J. Shipston, Nils Brose, and Robert H. Chow

From the Membrane Biology Group, Department of Biomedical Sciences, University of Edinburgh Medical School, Edinburgh EH8 9AG, United Kingdom and the  AG Molekulare Neurobiologie, Max-Planck-Institut für Experimentelle Medizin, Hermann-Rein Strasse 3, Göttingen D-37075, Germany

Munc13-1 and DOC2 have been implicated in the regulation of exocytosis. Here we demonstrate in vivo that these two proteins undergo a transient phorbol ester-mediated and protein kinase C-independent interaction, resulting in the translocation of DOC2 from a vesicular localization to the plasma membrane. The translocation of DOC2 is dependent upon the DOC2 Munc interacting domain that binds specifically to Munc13-1, whereas the association of DOC2 with intracellular membranes is dependent on its C2 domains. This is the first direct in vivo demonstration of a protein-protein interaction between two presynaptic proteins and may represent a molecular basis for phorbol ester-dependent enhancement of exocytosis.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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