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

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

Exploring the interactions between the Ca<sup>2+</sup> 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 presyna...

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Bibliographic Details
Main Authors: Christine Piotrowski, Rocco Moretti, Christian H. Ihling, André Haedicke, Thomas Liepold, Noa Lipstein, Jens Meiler, Olaf Jahn, Andrea Sinz
Format: Article
Language:English
Published: MDPI AG 2020-01-01
Series:Cells
Subjects:
munc13
calmodulin
cross-linking
mass spectrometry
protein<i>–</i>protein interaction
Online Access:https://www.mdpi.com/2073-4409/9/1/136

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https://www.mdpi.com/2073-4409/9/1/136

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