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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Physical and functional interactions of Doc2 and Munc13 in Ca2+-dependent exocytotic machinery.

Doc2 has two C2 domains that interact with Ca2+ and phospholipid. Munc13 has two C2 domains and one C1 domain that interacts with phorbol ester or diacylglycerol (DAG) and phospholipid. Both Doc2 and Munc13 are implicated in Ca2+-dependent neurotransmitter release, but their modes of action still remain unclear. We show here that Doc2 interacts with Munc13 both in a cell-free system and in intact PC12 cells during the high K+-induced Ca2+-dependent exocytosis. The Doc2- Munc13 interactions are stimulated by phorbol ester through the C1 domain of Munc13. Overexpression of the Doc2- interacting domain of Munc13 reduces the Ca2+-dependent exocytosis from PC12 cells, and co-expression with Doc2 suppresses this reduction. These results, together with the earlier findings that secretagogues produce DAG and elevate cytoplasmic Ca2+, suggest that the DAG-induced Doc2- Munc13 interactions play an important role in Ca2+-dependent exocytotic machinery.[1]

References

  1. Physical and functional interactions of Doc2 and Munc13 in Ca2+-dependent exocytotic machinery. Orita, S., Naito, A., Sakaguchi, G., Maeda, M., Igarashi, H., Sasaki, T., Takai, Y. J. Biol. Chem. (1997) [Pubmed]
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