In:
Biological Chemistry, Walter de Gruyter GmbH, Vol. 395, No. 7-8 ( 2014-7-1), p. 763-768
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.
Type of Medium:
Online Resource
ISSN:
1437-4315
,
1431-6730
DOI:
10.1515/hsz-2014-0134
Language:
English
Publisher:
Walter de Gruyter GmbH
Publication Date:
2014
detail.hit.zdb_id:
1466062-3
SSG:
12
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