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

Piotrowski, C.; Moretti, R.; Ihling, C. H.; Haedicke, A.; Liepold, T.; Lipstein, N.; Meiler, J.; Jahn, O.; Sinz, A.

doi:10.3390/cells9010136

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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

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Liepold, T.
Proteomics, Wiss. Servicegruppen, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Lipstein, N.
Molecular neurobiology, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Jahn, O.
Proteomics, Wiss. Servicegruppen, Max Planck Institute of Experimental Medicine, Max Planck Society;

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Citation

Piotrowski, C., Moretti, R., Ihling, C. H., Haedicke, A., Liepold, T., Lipstein, N., et al. (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: 136. doi:10.3390/cells9010136.

Cite as: https://hdl.handle.net/21.11116/0000-0007-4D1A-7

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.