Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Phosphorylation state-dependent interaction between AKAP7δ/γ and phospholamban increases phospholamban phosphorylation.

Cellular signalling - 1 Sept 2015

Rigatti Marc, Le Andrew V, Gerber Claire, Moraru Ion I, Dodge-Kafka Kimberly L

Abstract excerpt

Changes in heart rate and contractility in response to sympathetic stimulation occur via activation of cAMP dependent protein kinase A (PKA), leading to phosphorylation of numerous substrates that alter Ca(2+) cycling. Phosphorylation of these substrates is coordinated by A-kinase anchoring proteins (AKAPs), which recruit PKA to specific substrates [1]. Phosphorylation of the PKA substrate phospholamban (PLB) is...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Adaptor Proteins, Signal Transducing
Share to Calcium-Binding Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Cyclic AMP-Dependent Protein Kinases

Share to HEK293 Cells

Share to Phosphorylation

Share to Rats, Sprague-Dawley

Share to Sarcoplasmic Reticulum

Source

Open in PubMed Open full text

Identifiers

PMID: 26027516
DOI: 10.1016/j.cellsig.2015.05.016
PMCID: PMC4787601

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phosphorylation state-dependent interaction between AKAP7δ/γ and phospholamban increases phospholamban phosphorylation.PMID 26027516Read ↗

Structures of PKA-phospholamban complexes reveal a mechanism of familial dilated cardiomyopathySemantic proximity Read ↗

Dysfunctional conformational dynamics of protein kinase A induced by a lethal mutant of phospholamban hinder phosphorylation.Semantic proximity Read ↗

Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban.Semantic proximity Read ↗

Lethal, hereditary mutants of phospholamban elude phosphorylation by protein kinase A.Semantic proximity Read ↗

Phosphomimetic mutations increase phospholamban oligomerization and alter the structure of its regulatory complex.Semantic proximity Read ↗

Pathological mutations in the phospholamban cytoplasmic region affect its topology and dynamics modulating the extent of SERCA inhibition.Semantic proximity Read ↗

Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump.Semantic proximity Read ↗

Deception in simplicity: hereditary phospholamban mutations in dilated cardiomyopathy.Semantic proximity Read ↗

Protein Kinase A (PKA) Phosphorylation of Shp2 Protein Inhibits Its Phosphatase Activity and Modulates Ligand Specificity.Semantic proximity Read ↗

Polymorphisms/Mutations in A-Kinase Anchoring Proteins (AKAPs): Role in the Cardiovascular SystemSemantic proximity Read ↗

Mechanism of reversal of phospholamban inhibition of the cardiac Ca2+-ATPase by protein kinase A and by anti-phospholamban monoclonal antibody 2D12.Semantic proximity Read ↗

Protein kinase A and phosphodiesterase-4D3 binding to coding polymorphisms of cardiac muscle anchoring protein (mAKAP).Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.