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A minimal domain responsible for Munc13 activity


Munc13 proteins are essential in neurotransmitter release, controlling the priming of synaptic vesicles to a release-ready state. The sequences responsible for this priming activity are unknown. Here we identify a large α-helical domain of mammalian Munc13-1 that is autonomously folded and is sufficient to rescue the total arrest in neurotransmitter release observed in hippocampal neurons lacking Munc13s.

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Figure 1: Definition of the domain structure of rat Munc13-1.
Figure 2: The MUN domain rescues neurotransmitter release.


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We thank T. Südhof for fruitful discussions, H. Deng and R. Nehring for technical support and N. Brose (Max Planck Institute for Experimental Medicine, Gottingen, Germany) for providing the Munc13-1 and Munc13-2 double-knockout mice and the pSFV1-Munc13-1WT-EGFP vector. This work was supported by a grant from the Muscular Dystrophy Association and by US National Institutes of Health grants NS37200 to J.R. and NS51262 to C.R.

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Correspondence to Josep Rizo.

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The authors declare no competing financial interests.

Supplementary information

Supplementary Fig. 1

Munc13-1 fragments that did not fold (PDF 38 kb)

Supplementary Fig. 2

Secondary structure prediction of Munc13-1 (800-1579) (PDF 38 kb)

Supplementary Fig. 3

Purification of the MUN domain (PDF 18 kb)

Supplementary Fig. 4

The MUN domain does not bind syntaxin (PDF 137 kb)

Supplementary Methods

Computational analysis, cell culture and electrophysiology (PDF 28 kb)

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Basu, J., Shen, N., Dulubova, I. et al. A minimal domain responsible for Munc13 activity. Nat Struct Mol Biol 12, 1017–1018 (2005).

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