dc.contributor.author | Piotrowski, Christine | |
dc.contributor.author | Moretti, Rocco | |
dc.contributor.author | Ihling, Christian H. | |
dc.contributor.author | Haedicke, Andre | |
dc.contributor.author | Liepold, Thomas | |
dc.contributor.author | Lipstein, Noa | |
dc.contributor.author | Meiler, Jens | |
dc.contributor.author | Jahn, Olaf | |
dc.contributor.author | Sinz, Andrea | |
dc.date.accessioned | 2020-11-12T23:21:19Z | |
dc.date.available | 2020-11-12T23:21:19Z | |
dc.date.issued | 2020-01 | |
dc.identifier.citation | Piotrowski, C., Moretti, R., Ihling, C. H., Haedicke, A., Liepold, T., Lipstein, N., Meiler, J., Jahn, O., & Sinz, A. (2020). Delineating the Molecular Basis of the Calmodulin‒bMunc13-2 Interaction by Cross-Linking/Mass Spectrometry-Evidence for a Novel CaM Binding Motif in bMunc13-2. Cells, 9(1), 136. https://doi.org/10.3390/cells9010136 | en_US |
dc.identifier.other | eISSN: 2073-4409 | |
dc.identifier.uri | http://hdl.handle.net/1803/16287 | |
dc.description.abstract | Exploring the interactions between the Ca2+ binding protein calmodulin (CaM) and its target proteins remains a challenging task. Members of the Munc13 protein family play an essential role in short-term synaptic plasticity, modulated via the interaction with CaM at the presynaptic compartment. In this study, we focus on the bMunc13-2 isoform expressed in the brain, as strong changes in synaptic transmission were observed upon its mutagenesis or deletion. The CaM-bMunc13-2 interaction was previously characterized at the molecular level using short bMunc13-2-derived peptides only, revealing a classical 1-5-10 CaM binding motif. Using larger protein constructs, we have now identified for the first time a novel and unique CaM binding site in bMunc13-2 that contains an N-terminal extension of a classical 1-5-10 CaM binding motif. We characterize this motif using a range of biochemical and biophysical methods and highlight its importance for the CaM-bMunc13-2 interaction. | en_US |
dc.description.sponsorship | This research was funded by the DFG (project Si 867/15-2) and the region of Saxony-Anhalt. Work in the Meiler laboratory was supported through NIH NIGMS R01 GM080403 and GM073151. | en_US |
dc.language.iso | en_US | en_US |
dc.publisher | Cells | en_US |
dc.rights | Copyright © 2020 by the authors.
Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). | |
dc.source.uri | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7017353/ | |
dc.subject | Munc13 | en_US |
dc.subject | calmodulin | en_US |
dc.subject | cross-linking | en_US |
dc.subject | mass spectrometry | en_US |
dc.subject | protein-protein interaction | en_US |
dc.title | Delineating the Molecular Basis of the Calmodulin–bMunc13-2 Interaction by Cross-Linking/Mass Spectrometry—Evidence for a Novel CaM Binding Motif in bMunc13-2 | en_US |
dc.type | Article | en_US |
dc.identifier.doi | 10.3390/cells9010136 | |