Transient, phorbol ester-induced DOC2-Munc13 interactions in vivo

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

Research output: Contribution to journalArticlepeer-review

54 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)27347-27350
Number of pages4
JournalJournal of Biological Chemistry
Issue number39
Publication statusPublished - 24 Sept 1999


  • Alkaloids
  • Animals
  • Benzophenanthridines
  • Brain
  • Calcium-Binding Proteins
  • Cell Line
  • Cell Membrane
  • Enzyme Inhibitors
  • Exocytosis
  • Green Fluorescent Proteins
  • Humans
  • Intracellular Signaling Peptides and Proteins
  • Luminescent Proteins
  • Mice
  • Nerve Tissue Proteins
  • Open Reading Frames
  • Phenanthridines
  • Protein Kinase C
  • Rats
  • Recombinant Fusion Proteins
  • Tetradecanoylphorbol Acetate
  • Transfection


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