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 at Ser²⁶ in the ATP-binding site of Ca²⁺/calmodulin-dependent kinase II as a mechanism for switching off the kinase activity.

Bioscience reports - 7 Feb 2013

Yilmaz Mehtap, Gangopadhyay Samudra S, Leavis Paul, Grabarek Zenon, Morgan Kathleen G

Abstract excerpt

CaMKII (Ca²⁺/calmodulin-dependent kinase II) is a serine/threonine phosphotransferase that is capable of long-term retention of activity due to autophosphorylation at a specific threonine residue within each subunit of its oligomeric structure. The γ isoform of CaMKII is a significant regulator of vascular contractility. Here, we show that phosphorylation of CaMKII γ at Ser²⁶, a residue located within the...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphate
Share to Calcium

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Calcium-Calmodulin-Dependent Protein Kinase Type 2

Share to Calmodulin

Share to Ferrets

Share to Protein Isoforms

Share to Serine

Share to Threonine

Source

Open in PubMed Open full text

Identifiers

PMID: 23289753
DOI: 10.1042/BSR20120116
PMCID: PMC3566533

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Phosphorylation at Ser²⁶ in the ATP-binding site of Ca²⁺/calmodulin-dependent kinase II as a mechanism for switching off the kinase activity.PMID 23289753Read ↗

Interactions between αCaMKII and calmodulin in living cells: conformational changes arising from CaM-dependent and -independent relationships.Semantic proximity Read ↗

Phosphorylation sites in the Hook domain of CaVβ subunits differentially modulate CaV1.2 channel function.Semantic proximity Read ↗

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

Phosphorylation states greatly regulate the activity and gating properties of Cav 3.1 T-type Ca2+ channels.Semantic proximity Read ↗

Graded regulation of the Kv2.1 potassium channel by variable phosphorylation.Semantic proximity Read ↗

Decoding the Interactions Regulating the Active State Mechanics of Eukaryotic Protein Kinases.Semantic proximity Read ↗

Influence of a mutation in the ATP-binding region of Ca2+/calmodulin-dependent protein kinase II on its interaction with peptide substrates.Semantic proximity Read ↗

Potassium channel phosphorylation in excitable cells: providing dynamic functional variability to a diverse family of ion channels.Semantic proximity Read ↗

Widely Used CaMKII Regulatory Segment Mutations Cause Tight Actinin Binding and Dendritic Spine Enlargement in Unstimulated Neurons.Semantic proximity Read ↗

Glu60 of α-Calcium/calmodulin dependent protein kinase II mediates crosstalk between the regulatory T-site and protein substrate binding region of the active site.Semantic proximity Read ↗

Mitochondrial Protein Phosphorylation as a Regulatory Modality: Implications for Mitochondrial Dysfunction in Heart FailureSemantic proximity Read ↗

Casein kinase-mediated phosphorylation of serine 839 is necessary for basolateral localization of the Ca²⁺-activated non-selective cation channel TRPM4.Semantic proximity Read ↗

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