Details

Autor(en) / Beteiligte

• Piotrowski, Christine
• Moretti, Rocco
• Ihling, Christian H
• Haedicke, André
• Liepold, Thomas
• Lipstein, Noa
• Meiler, Jens
• Jahn, Olaf
• Sinz, Andrea

Titel

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

Ist Teil von

• Cells (Basel, Switzerland), 2020-01, Vol.9 (1), p.136

Ort / Verlag

Switzerland: MDPI AG

Erscheinungsjahr

2020

Quelle

MEDLINE

Beschreibungen/Notizen

• Exploring the interactions between the Ca 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 -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.