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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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Pull-down of Calmodulin-binding Proteins
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Human disease-associated calmodulin mutations alter calcineurin function through multiple mechanisms.

Ryan B Williams1, Md Nure Alam Afsar1, Svetlana Tikunova2

  • 1Department of Chemistry, Mississippi State University, Starkville MS 39759, U.S.A.

Cell Calcium
|May 28, 2023
PubMed
Summary

Disease-causing calmodulin (CaM) mutations impair calcineurin (CaN) function by altering CaM binding, calcium sensitivity, and kinetics. These CaN dysfunction mechanisms may contribute to calmodulinopathy, a severe heart disease.

Keywords:
Calcineurin (CaN)Calcium signalingHuman disease-associated calmodulin mutationsMechanisms of calmodulinopathy

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Cardiovascular Research

Background:

  • Calmodulin (CaM) is a crucial calcium-binding protein regulating numerous cellular processes.
  • Mutations in CaM cause calmodulinopathy, a life-threatening heart condition, linked to altered interactions with ion channels and kinases.
  • The impact of CaM mutations on other CaM-regulated proteins remains largely unexplored.

Purpose of the Study:

  • To investigate how disease-associated CaM mutations affect the function of calcineurin (CaN), a Ca2+-activated serine/threonine phosphatase.
  • To elucidate the biophysical and mechanistic basis of CaM mutation-induced CaN dysfunction.
  • To explore the potential contribution of altered CaN function to the pathogenesis of calmodulinopathy.

Main Methods:

  • Circular dichroism (CD) spectroscopy
  • Solution Nuclear Magnetic Resonance (NMR) spectroscopy
  • Stopped-flow kinetic measurements
  • Molecular Dynamics (MD) simulations
  • Biophysical characterization of CaN-CaM interactions

Main Results:

  • Specific CaM point mutations (N53I, F89L, D129G, F141L) were found to impair CaN phosphatase activity.
  • Mutations differentially affected CaM binding affinity, calcium (Ca2+) binding, and Ca2+ dissociation kinetics.
  • Structural analysis revealed alterations in the CaN-CaM complex, suggesting impaired allosteric signaling.
  • The degree of CaN inhibition varied among the tested CaM mutants.

Conclusions:

  • Disease-associated CaM mutations disrupt CaN function through diverse mechanisms.
  • Altered CaN activity due to CaM mutations represents a potential novel mechanism contributing to calmodulinopathy.
  • These findings expand our understanding of CaM's role in cardiovascular health and disease, highlighting CaN as a key player.