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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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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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Cyclic Adenosine Monophosphate (cAMP) is an essential second messenger that activates protein kinase A (PKA) and regulates various biological processes. A single epinephrine molecule binds to GPCR and activates several heterotrimeric G proteins, each stimulating multiple adenylyl cyclase, amplifying the signal, and synthesizing large numbers of cAMP molecules. Small changes in cAMP concentration affect PKA activity. The binding of four cAMP molecules induces a conformational change in PKA,...
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Pull-down of Calmodulin-binding Proteins
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Presynaptic Calmodulin targets: lessons from structural proteomics.

Noa Lipstein1, Melanie Göth2, Christine Piotrowski3

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

Expert Review of Proteomics
|February 23, 2017
PubMed
Summary
This summary is machine-generated.

Calmodulin (CaM) regulates synaptic transmission in neurons. This study identifies CaM targets in the presynaptic compartment using proteomic methods and discusses advanced structural techniques for characterizing these interactions.

Keywords:
CalmodulinMunc13chemical cross-linkingion mobilitymass spectrometryphotoaffinity labelingstructural proteomicssynapsesynaptic vesicle cycle

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Area of Science:

  • Neuroscience
  • Molecular Biology
  • Structural Biology

Background:

  • Calmodulin (CaM) is a crucial calcium-binding protein abundant in the brain.
  • In neurons, CaM translates calcium signals to regulate synaptic transmission.
  • Understanding CaM's presynaptic targets is key to synaptic function.

Purpose of the Study:

  • To review known and potential presynaptic CaM targets.
  • To present methods for identifying and characterizing CaM-Munc13 interactions.
  • To explore advanced techniques for CaM complex structural analysis.

Main Methods:

  • Literature review of CaM interactor screens.
  • Biochemical and structural proteomics workflow.
  • Ion mobility-mass spectrometry (IM-MS) and protein-protein cross-linking (PPX).

Main Results:

  • Established and candidate presynaptic CaM targets are outlined.
  • A workflow for CaM-Munc13 interaction characterization is presented.
  • Potential of IM-MS and PPX for CaM complex analysis is discussed.

Conclusions:

  • Advanced proteomic techniques like cross-linking/MS and native MS offer high-throughput analysis.
  • Combining cross-linking strategies provides robust experimental distance constraints.
  • Structural proteomics can yield CaM-insensitive mutants for functional studies.