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,...
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,...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Protein Kinases and Phosphatases02:54

Protein Kinases and Phosphatases

Proteins undergo chemical modifications that trigger changes in the charge, structure, and conformation of the proteins. Phosphorylation, acetylation, glycosylation, nitrosylation, ubiquitination, lipidation, methylation, and proteolysis are various protein modifications that regulate protein activity. Such modifications are usually enzyme-driven.
Protein kinases
Many proteins in the cell are regulated by phosphorylation, the addition of a phosphate group. A family of enzymes called kinases...
Amplifying Signals via Enzymatic Cascade01:22

Amplifying Signals via Enzymatic Cascade

When a ligand binds to a cell-surface receptor, the receptor's intracellular domain changes shape, which may either activate its enzyme function or allow its binding to other molecules. The initial signal is amplified by most signal transduction pathways. This means that a single ligand molecule can activate multiple molecules of a downstream target. Proteins that relay a signal are most commonly phosphorylated at one or more sites, activating or inactivating the protein. Kinases catalyze the...
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...

You might also read

Related Articles

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

Sort by
Same author

Mechanical thrombectomy for acute ischemic stroke in a low- and middle-income country: primary outcomes from the GRASSROOT Trial.

Journal of neurointerventional surgery·2025
Same author

Factors Contributing to Low Utilization of Intracoronary Imaging in Clinical Practice: A White Paper.

Journal of the Society for Cardiovascular Angiography & Interventions·2025
Same author

A Fork at the End of the Road.

JACC. Cardiovascular interventions·2025
Same author

Management of Coronary Stent Underexpansion.

Journal of the American College of Cardiology·2025
Same author

Systematic Review and Meta-Analysis of the Super High-Pressure Balloon (SIS-OPN) for Percutaneous Coronary Intervention.

Catheterization and cardiovascular interventions : official journal of the Society for Cardiac Angiography & Interventions·2025
Same author

Coronary artery disease and percutaneous coronary intervention in patients with severe chronic kidney disease.

Progress in cardiovascular diseases·2025

Related Experiment Video

Updated: Jun 22, 2026

Primary Culture of Adult Rat Heart Myocytes
11:44

Primary Culture of Adult Rat Heart Myocytes

Published on: June 16, 2009

Protein kinase C isoforms differentially phosphorylate Ca(v)1.2 alpha(1c).

Lin Yang1, Darshan Doshi, John Morrow

  • 1Division of Cardiology, Department of Medicine, College of Physicians and Surgeons,Columbia University, New York, New York 10032, USA.

Biochemistry
|June 17, 2009
PubMed
Summary

Protein kinase C (PKC) phosphorylates the L-type calcium channel (Ca(v)1.2) at specific sites, influencing heart function. Different PKC isoforms target distinct sites, offering a mechanism for varied effects on cardiac contractility.

More Related Videos

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Related Experiment Videos

Last Updated: Jun 22, 2026

Primary Culture of Adult Rat Heart Myocytes
11:44

Primary Culture of Adult Rat Heart Myocytes

Published on: June 16, 2009

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay
12:26

Identification of Cyclin-dependent Kinase 1 Specific Phosphorylation Sites by an In Vitro Kinase Assay

Published on: May 3, 2018

Area of Science:

  • Cardiovascular Physiology
  • Molecular Biology
  • Biochemistry

Background:

  • Regulation of calcium (Ca2+) influx via L-type Ca2+ channels (Ca(v)1.2) is crucial for cardiac excitation-contraction coupling.
  • Ca(v)1.2 channels are implicated in signaling pathways of the renin-angiotensin and sympathetic nervous systems.
  • Limited biochemical data exists on the specific protein phosphorylation events regulating Ca(v)1.2.

Purpose of the Study:

  • To identify and characterize protein kinase C (PKC) phosphorylation sites on the alpha(1c) subunit of Ca(v)1.2.
  • To investigate the differential phosphorylation of Ca(v)1.2 by various PKC isoforms.
  • To elucidate the molecular mechanisms underlying PKC-mediated modulation of cardiac contractility.

Main Methods:

  • Identification of seven novel PKC phosphorylation sites within the alpha(1c) subunit.
  • Utilized phospho-epitope specific antibodies to detect phosphorylation at Ser(1674) and Ser(1928) in HEK cells and rat hearts.
  • Employed PMA to induce phosphorylation and bisindolylmaleimide as a PKC inhibitor.

Main Results:

  • Both Ser(1674) and Ser(1928) in the Ca(v)1.2 C-terminus are phosphorylated in response to PMA in HEK cells and rat hearts.
  • Phosphorylation at Ser(1674) is dependent on specific PKC isoforms (PKCα, βI, βII, γ, δ, θ), while Ser(1928) is targeted by a broader range.
  • Demonstrated that PKC isoform specificity in phosphorylation contributes to differential effects on Ca(v)1.2 channel activity.

Conclusions:

  • Identified multiple PKC phosphorylation sites on the Ca(v)1.2 alpha(1c) subunit, expanding our understanding of its regulation.
  • Established that distinct PKC isoforms phosphorylate specific residues (Ser1674 vs. Ser1928), providing a mechanism for isoform-specific modulation of cardiac function.
  • These findings offer molecular insights into how PKC signaling pathways differentially impact cardiac contractility and relaxation.