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Related Concept Videos

Calmodulin-dependent Signaling01:16

Calmodulin-dependent Signaling

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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GPCRs Regulate Adenylyl Cylase Activity01:09

GPCRs Regulate Adenylyl Cylase Activity

Some GPCRs transmit signals through adenylyl cyclase (AC), a transmembrane enzyme. AC helps synthesize second messenger cyclic adenosine monophosphate (cAMP). AC catalyzes cyclization reaction and converts ATP to cAMP by releasing a pyrophosphate. The pyrophosphate is further hydrolyzed to phosphate by the enzyme pyrophosphatase, which drives cAMP synthesis to completion. However, cAMP is rapidly degraded to 5′ AMP by the enzymes phosphodiesterase (PDE), preventing overstimulation of cells.
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Structure of Cadherins01:25

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

Structural insights into calmodulin/adenylyl cyclase 8 interaction.

Sabine Herbst1, Nana Masada, Sabrina Pfennig

  • 1Department of Pharmaceutical Chemistry and Bioanalytics, Institute of Pharmacy, Martin-Luther University Halle-Wittenberg, Wolfgang-Langenbeck-Str. 4, 06120, Halle, Germany.

Analytical and Bioanalytical Chemistry
|September 28, 2013
PubMed
Summary

Calmodulin (CaM) binding to adenylyl cyclase 8 (AC8) involves CaM adopting a collapsed structure around AC8 peptides. This study reveals CaM does not bind both AC8 peptides simultaneously, clarifying Ca(2+) signaling mechanisms.

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Cell Signaling

Background:

  • Calmodulin (CaM) is a crucial Ca(2+)-binding protein regulating numerous cellular processes.
  • Adenylyl cyclases (ACs) synthesize cAMP, a key second messenger, and are regulated by CaM, linking Ca(2+) and cAMP signaling.
  • AC8's regulation by CaM involves specific binding mechanisms that require further structural elucidation.

Purpose of the Study:

  • To investigate the structural mechanisms of CaM regulation by AC8.
  • To determine how CaM interacts with the CaM-binding regions of AC8.
  • To refine the understanding of Ca(2+) signaling pathways involving CaM and AC8.

Main Methods:

  • Utilized chemical cross-linking and mass spectrometry to analyze CaM/AC8 peptide complexes.
  • Employed isothermal titration calorimetry to thermodynamically investigate AC8 peptide binding to CaM.
  • Focused on two peptides representing the CaM-binding regions of AC8.

Main Results:

  • CaM/AC8 peptide complex structures resemble the CaM/skeletal muscle myosin light chain kinase complex, with CaM collapsed around the peptide.
  • AC8 peptides bind CaM in an antiparallel orientation.
  • No evidence was found for simultaneous binding of both AC8 peptides to a single CaM molecule.

Conclusions:

  • The interaction of CaM with AC8 peptides involves a 'collapsed' CaM structure.
  • The findings refine the understanding of CaM-AC8 interaction, indicating a 1:1 binding stoichiometry for these specific peptides.
  • This work contributes to understanding the diverse regulatory mechanisms of CaM-stimulated AC isoforms.