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Pull-down of Calmodulin-binding Proteins
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Published on: January 23, 2012

Nonconserved Ca(2+)/calmodulin binding sites in Munc13s differentially control synaptic short-term plasticity.

Noa Lipstein1, Sabine Schaks, Kalina Dimova

  • 1Department of Molecular Neurobiology, Max Planck Institute of Experimental Medicine, Göttingen, Germany.

Molecular and Cellular Biology
|September 12, 2012
PubMed
Summary

Calcium/calmodulin binding enhances synaptic vesicle priming by Munc13-2 and Munc13-3, increasing neurotransmission. This Ca(2+)/calmodulin regulation is conserved across Munc13 isoforms, influencing short-term synaptic plasticity.

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Cell Biology

Background:

  • Munc13 proteins are crucial for synaptic vesicle priming, controlling the readily releasable pool.
  • Munc13-1 and ubMunc13-2 bind Ca(2+)/calmodulin during high activity, enhancing priming and altering synaptic plasticity.
  • Neuronal subtype-specific Munc13 isoforms, bMunc13-2 and Munc13-3, have distinct expression patterns.

Purpose of the Study:

  • To investigate if bMunc13-2 and Munc13-3 mediate synaptic vesicle priming and regulate short-term synaptic plasticity in a Ca(2+)/calmodulin-dependent manner.
  • To determine the structural basis for Ca(2+)/calmodulin interaction with Munc13 isoforms.
  • To compare the functional regulation of priming by different Munc13 isoforms.

Main Methods:

  • Identification of functional Ca(2+)/calmodulin binding sites in bMunc13-2 and Munc13-3.
  • Structural analysis of Munc13-calmodulin interactions.
  • Electrophysiological analysis of synaptic activity and vesicle priming.

Main Results:

  • A single functional Ca(2+)/calmodulin binding site was identified in bMunc13-2 and Munc13-3.
  • Structural evidence suggests a conserved mode of calmodulin interaction across Munc13s, despite sequence divergence.
  • Ca(2+)/calmodulin binding positively regulates priming activity of bMunc13-2 and Munc13-3 during high-frequency activity.
  • This regulation increases the readily releasable pool size and enhances short-term synaptic transmission.

Conclusions:

  • Ca(2+)/calmodulin-dependent regulation of synaptic vesicle priming is structurally and functionally conserved across all Munc13 proteins.
  • The specific composition of Munc13 isoforms in a neuron differentially modulates its short-term synaptic plasticity characteristics.