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- W2327974773 abstract "Munc13 proteins are essential presynaptic regulators that mediate synaptic vesicle priming and play a role in the regulation of neuronal short-term synaptic plasticity. All four Munc13 isoforms share a common domain structure, including a calmodulin (CaM) binding site in their otherwise divergent N-termini. Here, we summarize recent results on the investigation of the CaM/Munc13 interaction. By combining chemical cross-linking, photoaffinity labeling, and mass spectrometry, we showed that all neuronal Munc13 isoforms exhibit similar CaM binding modes. Moreover, we demonstrated that the 1-5-8-26 CaM binding motif discovered in Munc13-1 cannot be induced in the classical CaM target skMLCK, indicating unique features of the Munc13 CaM binding motif." @default.
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- W2327974773 date "2014-04-17" @default.
- W2327974773 modified "2023-10-01" @default.
- W2327974773 title "Structural insights into calmodulin/Munc13 interaction" @default.
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- W2327974773 doi "https://doi.org/10.1515/hsz-2014-0134" @default.
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