Synapse
⌘+K
Synapse
PulseExploreClubsResearchersJournals
Instagram
HomeClubsExplore
September 11, 2014AJP Cell Physiology

A new phosphorylation site in cardiac L-type Ca2+ channels (Cav1.2) responsible for its cAMP-mediated modulation

View Full Paper
Ask AI
Bookmark
Share

Key result

Mutation of Ser1574 (C1 site) abolished forskolin-mediated enhancement of Cav1.2 channel activity, suggesting it is a potential site for PKA-mediated modulation.

Population

Guinea pig Cav1.2 Ca(2+) channel (wild-type and mutants) and peptides of the COOH-terminal tail of α1C

Comparison

Mutation of potential phosphorylation sites and… vs Wild-type Ca(2+) channel and unmutated peptides

Design

Preclinical

Authors

EMEtsuko MinobeKagoshima UniversitySMSachiko MaedaSaga UniversityJXJianjun XuKagoshima University

Discussion

Loading...

Member takes

Implication

Hypothesis-generating for PKA regulation of cardiac Cav1.2; leaves open physiological relevance pending in vivo validation.

Structured PICO

P
Population
Guinea pig Cav1.2 Ca(2+) channel (wild-type and mutants) and peptides of the COOH-terminal tail of α1C
I
Intervention
Mutation of potential phosphorylation sites (S1574A, S1626A, S1699A, T1908A, S1927A) and exposure to adenylyl cyclase activator forskolin (Fsk, 5 μM) or PKA
C
Comparator
Wild-type Ca(2+) channel and unmutated peptides
O
Outcome
Ca(2+) channel activity modulation by forskolin and in vitro phosphorylation by PKAsurrogate

Ser(1574) in the carboxyl terminal region of the α1C-subunit of the cardiac L-type Ca2+ channel is identified as a potential key site for PKA-mediated modulation.

Cite This Study

Minobe et al. (2014) studied this question. Mutation of potential phosphorylation sites (e.g., S1574A) vs. Wild-type Ca(2+) channel was evaluated on Channel activity modulation by forskolin and phosphorylation by PKA. Mutation of Ser1574 (C1 site) abolished forskolin-mediated enhancement of Cav1.2 channel activity, suggesting it is a potential site for PKA-mediated modulation.

synapsesocial.com/papers/6a21cbee4c1bee377cecaea6https://doi.org/10.1152/ajpcell.00267.2014
View Full Paper
Ask AI
Bookmark
Share

Also Consider

Synapse has enriched 5 closely related papers on similar clinical questions. Consider them for comparative context:

  1. 1Cloning and Expression of the Ca2+ Channel 1c and 2a Subunits from Guinea Pig Heart1999 · 12 citations
  2. 2β-Adrenergic Stimulation of L-type Ca 2+ Channels in Cardiac Myocytes Requires the Distal Carboxyl Terminus of α 1C but Not Serine 19282006 · 134 citations
  3. 3β-Adrenergic Regulation of the L-type Ca 2+ Channel Does Not Require Phosphorylation of α 1C Ser 17002013 · 57 citations
  4. 4β-Adrenergic regulation requires direct anchoring of PKA to cardiac Ca V 1.2 channels via a leucine zipper interaction with A kinase-anchoring protein 152003 · 230 citations
  5. 5Specific Phosphorylation of a Site in the Full-Length Form of the α1 Subunit of the Cardiac L-Type Calcium Channel by Adenosine 3‘,5‘-Cyclic Monophosphate- Dependent Protein Kinase1996 · 284 citations