Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Experiment Videos

Intracellular coupling via limiting calmodulin.

Quang-Kim Tran1, D J Black, Anthony Persechini

  • 1Division of Molecular Biology & Biochemistry, School of Biological Sciences, University of Missouri, Kansas City 64110-2499, USA.

The Journal of Biological Chemistry
|May 10, 2003
PubMed
Summary
This summary is machine-generated.

Related Concept Videos

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

A perilysosomal feedforward mechanism regulates starvation-induced calcium signaling.

The FEBS journal·2026
Same author

Available CALM (calmodulin) and autophagy: pas de deux at rest.

Autophagy reports·2025
Same author

The three calmodulin genes: territories defined?

Cardiovascular research·2025
Same author

Promotion of nitric oxide production: mechanisms, strategies, and possibilities.

Frontiers in physiology·2025
Same author

Regulation of basal autophagy by calmodulin availability.

The FEBS journal·2022
Same author

Endothelial regulation of calmodulin expression and eNOS-calmodulin interaction in vascular smooth muscle.

Molecular and cellular biochemistry·2022
Same journal

Correction: Characterization of Mast2 kinase defines structural features, regulation, and substrates.

The Journal of biological chemistry·2026
Same journal

Isotope-Edited ESEEM: A New Method for Probing Copper Binding Sites in Neurodegenerative Proteins.

The Journal of biological chemistry·2026
Same journal

Introduction to the Thematic Review Series on Intracellular Protein Degradation. The ubiquitous biology of intracellular protein degradation: a tribute to Alfred L. ("Fred") Goldberg.

The Journal of biological chemistry·2026
Same journal

Correction: Aromatic residue-rich amino-terminal segments of temporin L self-assemble into collagen-mimetic peptides with cell-adhesion properties.

The Journal of biological chemistry·2026
Same journal

YhbO is a DJ-1 family glyoxalase and α-oxoaldehyde hydratase that confers resistance to reactive carbonyl stress (112).

The Journal of biological chemistry·2026
Same journal

ARMH3 acts as a central scaffold at the Golgi/TGN through interactions with Arl5, GBF1, and PI4KB.

The Journal of biological chemistry·2026
See all related articles

Competition for calmodulin links cellular processes. Increased nitric-oxide synthase activity reduces available calmodulin, decreasing other calmodulin-dependent activities like the plasma membrane Ca2+ pump.

Area of Science:

  • Cellular biology
  • Biochemistry
  • Physiology

Background:

  • Cellular Ca2+-calmodulin concentrations suggest competition for calmodulin may link calmodulin-dependent activities.
  • Endothelial cells utilize calmodulin to regulate various cellular functions.

Purpose of the Study:

  • To directly test the hypothesis that competition for limiting calmodulin couples calmodulin-dependent activities.
  • To investigate the relationship between nitric-oxide synthase activity, calmodulin binding, and downstream cellular effects.

Main Methods:

  • Quantitative immunoblotting to determine calmodulin binding to nitric-oxide synthase.
  • Simultaneous determination of free Ca2+ and Ca2+-calmodulin concentrations using indo-1 and a fluorescent calmodulin biosensor.
  • Assessing calmodulin-dependent plasma membrane Ca2+ pump activity.

Related Experiment Videos

Main Results:

  • Increased nitric-oxide synthase activity (3-fold) correlated with increased calmodulin binding (up to 25% of total cellular calmodulin).
  • Increased calmodulin binding to nitric-oxide synthase led to reduced Ca2+-calmodulin concentrations and increased [Ca2+]50 for biosensor complex formation.
  • A 40% reduction in calmodulin-dependent plasma membrane Ca2+ pump activity was observed, directly linked to reduced calmodulin availability.

Conclusions:

  • Increases in nitric-oxide synthase activity are coupled to decreases in other calmodulin targets via depletion of a limited calmodulin pool.
  • This mechanism of calmodulin availability likely serves as a ubiquitous method for coupling diverse calmodulin-dependent activities within the cell.