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Structural insights into calmodulin/Munc13 interaction.
- Source :
-
Biological chemistry [Biol Chem] 2014 Jul; Vol. 395 (7-8), pp. 763-8. - Publication Year :
- 2014
-
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.
Details
- Language :
- English
- ISSN :
- 1437-4315
- Volume :
- 395
- Issue :
- 7-8
- Database :
- MEDLINE
- Journal :
- Biological chemistry
- Publication Type :
- Academic Journal
- Accession number :
- 24854537
- Full Text :
- https://doi.org/10.1515/hsz-2014-0134