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Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
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The cadherins were one of the first cell adhesion molecules discovered; the term “cadherins”   is based on their calcium-dependent adhering properties. The first cadherins discovered on the epithelial, neuronal, and placental cells were named E-cadherin, P-cadherin, and N-cadherin, respectively. These classical cadherins share sequence and structural similarities. Other cadherins, including those involved in cell signaling, are grouped into non-classical cadherins. This...
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Pull-down of Calmodulin-binding Proteins
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Structural insights into calmodulin/Munc13 interaction.

Sabine Herbst, Noa Lipstein, Olaf Jahn

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    Summary
    This summary is machine-generated.

    Munc13 proteins regulate synaptic vesicle priming and plasticity. This study reveals unique calmodulin binding modes across Munc13 isoforms, distinct from other calmodulin targets.

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    Area of Science:

    • Neuroscience
    • Molecular Biology
    • Biochemistry

    Background:

    • Munc13 proteins are crucial presynaptic regulators.
    • They control synaptic vesicle priming and short-term synaptic plasticity.
    • All Munc13 isoforms possess a calmodulin (CaM) binding site in their N-termini.

    Purpose of the Study:

    • To investigate the interaction between calmodulin and Munc13 isoforms.
    • To characterize the CaM binding modes in neuronal Munc13 proteins.

    Main Methods:

    • Utilized chemical cross-linking.
    • Employed photoaffinity labeling.
    • Applied mass spectrometry.

    Main Results:

    • All neuronal Munc13 isoforms demonstrated similar calmodulin binding modes.
    • The unique 1-5-8-26 CaM binding motif found in Munc13-1 could not be replicated in skMLCK.
    • This suggests unique characteristics of the Munc13 CaM binding motif.

    Conclusions:

    • Calmodulin interacts with neuronal Munc13 isoforms through conserved binding modes.
    • Munc13 proteins exhibit unique calmodulin binding properties compared to classical targets.