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,...
Feedback Regulation of Calcium Concentration01:27

Feedback Regulation of Calcium Concentration

Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
IP3/DAG Signaling Pathway01:11

IP3/DAG Signaling Pathway

Membrane lipids such as phosphatidylinositol (PI) are precursors for several membrane-bound and soluble second messengers. Specific kinases phosphorylate PI and produce phosphorylated inositol phospholipids. One such inositol phospholipids are the  phosphatidylinositol-4,5 bisphosphate [PI(4,5)P2], present in the inner half of the lipid bilayer. Upon ligand binding, GPCR stimulates Gq proteins to turn on phospholipase Cꞵ. Activated phospholipase Cꞵ cleaves PI(4,5)P2 and produces two-second...
cAMP-dependent Protein Kinase Pathways01:25

cAMP-dependent Protein Kinase Pathways

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,...
Amplifying Signals via Second Messengers01:15

Amplifying Signals via Second Messengers

Many receptor binding ligands are hydrophilic; they do not cross the cell membrane but bind to cell-surface receptors. Thus, their message must be relayed by second messengers present in the cell cytoplasm. There are several second messenger pathways, each with its own way of relaying information. For example, the G protein-coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol pathway is active when the receptor induces...
What are Second Messengers?01:12

What are Second Messengers?

Because many receptor binding ligands are hydrophilic, they do not cross the cell membrane and thus their message must be relayed to a second messenger on the inside. There are several second messenger pathways, each with their own way of relaying information. G-protein coupled receptors can activate both phosphoinositol and cyclic AMP (cAMP) second messenger pathways. The phosphoinositol path is active when the receptor induces phospholipase C to hydrolyze the phospholipid,...

You might also read

Related Articles

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

Sort by
Same author

Graduate Students Find Content of Responsible Conduct of Research Coursework Useful.

Science and engineering ethics·2026
Same author

Efficacy of Centers of Biomedical Research Excellence (CoBRE) grants to build research capacity in underrepresented states.

FASEB journal : official publication of the Federation of American Societies for Experimental Biology·2024
Same author

Training doctoral students in critical thinking and experimental design using problem-based learning.

BMC medical education·2023
Same author

Efficacy of Centers of Biomedical Research Excellence (CoBRE) Grants to Build Research Capacity in Underrepresented States.

bioRxiv : the preprint server for biology·2023
Same author

Research productivity and training support for doctoral students in the biological and biomedical sciences.

FASEB bioAdvances·2023
Same author

Introducing conflict resolution and negotiation training into a biomedical sciences graduate curriculum.

BMC medical education·2022

Related Experiment Video

Updated: Jul 7, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Calcium-dependent Pyk2 activation: a role for calmodulin?

Michael D Schaller1

  • 1Lineberger Comprehensive Cancer Center, Carolina Cardiovascular Biology Center, Comprehensive Center for Inflammatory Disorders, 534 Taylor Hall, CB 7090, University of North Carolina, Chapel Hill, NC 5799, USA. email crispy4@med.unc.edu

The Biochemical Journal
|February 23, 2008
PubMed
Summary
This summary is machine-generated.

Calcium signals activate proline-rich tyrosine kinase 2 (Pyk2) by binding calmodulin to its FERM domain. This study provides the first mechanistic insight into calcium-dependent Pyk2 regulation, crucial for understanding cellular responses.

More Related Videos

Fluorescent Calcium Imaging and Subsequent In Situ Hybridization for Neuronal Precursor Characterization in Xenopus laevis
09:07

Fluorescent Calcium Imaging and Subsequent In Situ Hybridization for Neuronal Precursor Characterization in Xenopus laevis

Published on: February 18, 2020

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading (TED)
09:32

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading (TED)

Published on: May 7, 2013

Related Experiment Videos

Last Updated: Jul 7, 2026

Pull-down of Calmodulin-binding Proteins
07:51

Pull-down of Calmodulin-binding Proteins

Published on: January 23, 2012

Fluorescent Calcium Imaging and Subsequent In Situ Hybridization for Neuronal Precursor Characterization in Xenopus laevis
09:07

Fluorescent Calcium Imaging and Subsequent In Situ Hybridization for Neuronal Precursor Characterization in Xenopus laevis

Published on: February 18, 2020

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading (TED)
09:32

Direct Imaging of ER Calcium with Targeted-Esterase Induced Dye Loading (TED)

Published on: May 7, 2013

Area of Science:

  • Biochemistry
  • Cell Biology
  • Molecular Signaling

Background:

  • Proline-rich tyrosine kinase 2 (Pyk2) and focal adhesion kinase (FAK) are related tyrosine kinases.
  • Pyk2 and FAK exhibit differential regulation in response to cytoplasmic calcium levels.
  • Understanding calcium-dependent enzyme activation is critical in cellular signaling.

Purpose of the Study:

  • To elucidate the mechanism of calcium-dependent regulation of Pyk2.
  • To investigate the role of calmodulin in Pyk2 activation.
  • To explore the interaction between calcium signals and Pyk2 activity.

Main Methods:

  • Biochemical assays to study protein-protein interactions.
  • Analysis of Pyk2 activation in response to calcium signaling.
  • Investigating the role of the FERM domain in Pyk2 regulation.

Main Results:

  • Calmodulin binding to the FERM domain of Pyk2 promotes enzyme activation.
  • Vasopressin-triggered calcium signals mediate Pyk2 activation via calmodulin.
  • This study offers the first mechanistic insight into Pyk2 regulation by calcium.

Conclusions:

  • Calmodulin is a key mediator in the calcium-dependent activation of Pyk2.
  • The FERM domain is implicated in the calmodulin-Pyk2 interaction.
  • These findings advance the understanding of calcium signaling pathways and tyrosine kinase regulation.