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 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.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Proteomics01:33

Proteomics

A proteome is the entire set of proteins that a cell type produces. We can study proteomes using the knowledge of genomes because genes code for mRNAs, and the mRNAs encode proteins. Although mRNA analysis is a step in the right direction, not all mRNAs are translated into proteins.
Proteomics is the study of proteomes' function. It involves the large-scale systematic study of the proteome to denote the protein complement expressed by a genome. Scientist Mark Wilkins coined the term proteomics...
Protein Networks02:26

Protein Networks

An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...

You might also read

Related Articles

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

Sort by
Same author

High-resolution structure of monomorphic Aβ<sub>1-40</sub> fibrils.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

The chaperone DNAJB6b halts amyloid formation through association with transient Aβ oligomers.

Physical chemistry chemical physics : PCCP·2026
Same author

The temperature dependence of amyloid <i>β</i> solubility reveals the hydrophobic effect as the main driving force for fibril formation.

Proceedings of the National Academy of Sciences of the United States of America·2026
Same author

Rapid elongation drives the exceptionally fast aggregation of the most common localized human amyloid medin.

Communications chemistry·2026
Same author

Transient Interactions of α-Synuclein N- and C-Termini.

ACS chemical neuroscience·2026
Same author

Correction to "Design of Tau Aggregation Inhibitors Using Iterative Machine Learning and a Polymorph-Specific Brain-Seeded Fibril Amplification Assay".

Journal of the American Chemical Society·2026

Related Experiment Video

Updated: May 29, 2026

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

Probing calmodulin protein-protein interactions using high-content protein arrays.

David J O'Connell1, Mikael Bauer, Sara Linse

  • 1Conway Institute of Biomolecular & Biomedical Research, University College Dublin, Dublin, Ireland.

Methods in Molecular Biology (Clifton, N.J.)
|September 9, 2011
PubMed
Summary

Calcium ion (Ca2+) is vital for cell signaling, regulated by proteins like calmodulin. Researchers discovered calmodulin binds strongly to STIM1 and STIM2, key proteins in calcium entry into cells.

More Related Videos

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
06:01

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Published on: January 7, 2019

Related Experiment Videos

Last Updated: May 29, 2026

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions
06:01

Extracellular Protein Microarray Technology for High Throughput Detection of Low Affinity Receptor-Ligand Interactions

Published on: January 7, 2019

Area of Science:

  • Cellular Biology
  • Biochemistry
  • Molecular Biology

Background:

  • Calcium ion (Ca2+) acts as a critical second messenger regulating diverse cellular functions.
  • Intracellular Ca2+-binding proteins, notably calmodulin, mediate Ca2+ signals.
  • Calmodulin is essential for cellular responses to stimuli that increase cytosolic Ca2+ concentration.

Purpose of the Study:

  • To identify novel protein-protein interactions involving calmodulin.
  • To investigate calmodulin's role in cellular calcium regulation pathways.

Main Methods:

  • Utilized a high-content recombinant human protein array.
  • Probed the array with fluorophore-labeled calmodulin in the presence of Ca2+.
  • Screened over 10,000 unique human proteins from a human brain cDNA library.

Main Results:

  • Identified a high-affinity interaction between calmodulin and STIM1.
  • Identified a high-affinity interaction between calmodulin and STIM2.
  • STIM1 and STIM2 are single-pass transmembrane proteins localized to the endoplasmic reticulum.

Conclusions:

  • Calmodulin directly interacts with STIM1 and STIM2.
  • This interaction is significant for the translocation of STIM1/STIM2 to the plasma membrane.
  • The findings shed light on the regulation of store-operated calcium entry.