Structural insights into calmodulin/Munc13 interaction
| Autor: | Noa Lipstein, Sabine Herbst, Olaf Jahn, Andrea Sinz |
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| Rok vydání: | 2014 |
| Předmět: |
Models
Molecular Gene isoform Photoaffinity labeling Calmodulin biology Protein Conformation Chemistry Clinical Biochemistry Nerve Tissue Proteins Plasma protein binding Biochemistry Cell biology Protein structure Synaptic plasticity biology.protein Humans Binding site Molecular Biology Synaptic vesicle priming Protein Binding |
| Zdroj: | Biological Chemistry. 395:763-768 |
| ISSN: | 1437-4315 1431-6730 |
| DOI: | 10.1515/hsz-2014-0134 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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