Identification of a novel cAMP dependent protein kinase A phosphorylation site on the human cardiac calcium channel

Henrietta Cserne Szappanos1, Padmapriya Muralidharan1, Evan Ingley2,3

  • 1School of Human Sciences, University of Western Australia, Crawley, Western Australia, Australia.

Scientific Reports
|November 11, 2017
PubMed

Insights

The "Fight or Flight" response requires cardiac calcium channels. Researchers identified a novel PKA phosphorylation site (Ser1458) on the Cav1.2 channel, crucial for increased calcium influx during stress.

Area of Science:

  • Cardiovascular Physiology
  • Molecular Biology
  • Cell Signaling

Background:

  • The
  • Fight or Flight

Purpose of the Study:

  • Identify the specific PKA phosphorylation site on the cardiac L-type Ca2+ channel (Cav1.2) involved in the
  • Fight or Flight

Main Methods:

  • Cell-free system with purified Cav1.2 channel protein reconstituted in proteoliposomes
  • Assessed channel open probability
  • Utilized fluorescent phosphoprotein detection and MS/MS mass spectrometry

Main Results:

  • Identified Ser1458 as the novel PKA phosphorylation site on the Cav1.2 α1 subunit
  • Phosphorylation at Ser1458 increased channel opening frequency
  • This site is near the Repeat IV S6 region and induces a conformational change

Conclusions:

  • Phosphorylation of Cav1.2 at Ser1458 is necessary and sufficient for increased calcium influx
  • This finding elucidates a key mechanism in the
  • Fight or Flight

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,...
6.6K
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,...
8.6K
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...
15.3K