Alpha-kinase anchoring protein alphaKAP interacts with SERCA2A to spatially position Ca2+/calmodulin-dependent protein kinase II and modulate phospholamban phosphorylation (Q42077393)

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English	Alpha-kinase anchoring protein alphaKAP interacts with SERCA2A to spatially position Ca2+/calmodulin-dependent protein kinase II and modulate phospholamban phosphorylation	scientific article

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scholarly article

1 reference

Europe PubMed Central

PMC publication ID

16 October 2017

Alpha-kinase anchoring protein alphaKAP interacts with SERCA2A to spatially position Ca2+/calmodulin-dependent protein kinase II and modulate phospholamban phosphorylation (English)

1 reference

Europe PubMed Central

PMC publication ID

16 October 2017

phosphorylation

0 references

author name string

Puneet Singh

1

1 reference

Europe PubMed Central

PMC publication ID

16 October 2017

Maysoon Salih

2

1 reference

Europe PubMed Central

PMC publication ID

16 October 2017

Balwant S Tuana

3

1 reference

Europe PubMed Central

PMC publication ID

16 October 2017

language of work or name

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publication date

11 August 2009

1 reference

Europe PubMed Central

PMC publication ID

16 October 2017

Journal of Biological Chemistry

1 reference

Europe PubMed Central

PMC publication ID

16 October 2017

284

1 reference

Europe PubMed Central

PMC publication ID

16 October 2017

41

1 reference

Europe PubMed Central

PMC publication ID

16 October 2017

28212-28221

1 reference

Europe PubMed Central

PMC publication ID

16 October 2017

Requirement for Ca2+/calmodulin-dependent kinase II in the transition from pressure overload-induced cardiac hypertrophy to heart failure in mice.

1 reference

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Calmodulin-kinases: modulators of neuronal development and plasticity

1 reference

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30 May 2018

Phosphorylation of the cAMP-dependent protein kinase (PKA) regulatory subunit modulates PKA-AKAP interaction, substrate phosphorylation, and calcium signaling in cardiac cells

1 reference

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AKAP complex regulates Ca2+ re-uptake into heart sarcoplasmic reticulum

1 reference

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Early cardiac hypertrophy in mice with impaired calmodulin regulation of cardiac muscle Ca release channel

1 reference

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Calmodulin and CaMKII as molecular switches for cardiac ion channels.

1 reference

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Regulation of sodium and calcium channels by signaling complexes

1 reference

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AKAP signaling complexes: getting to the heart of the matter

1 reference

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The where's and when's of kinase anchoring

1 reference

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Distinct enzyme combinations in AKAP signalling complexes permit functional diversity

1 reference

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Role of phospholamban phosphorylation on Thr17 in cardiac physiological and pathological conditions

1 reference

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Alternative splicing generates a CaM kinase IIbeta isoform in myocardium that targets the sarcoplasmic reticulum through a putative alphaKAP and regulates GAPDH.

1 reference

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Beta-adrenergic regulation requires direct anchoring of PKA to cardiac CaV1.2 channels via a leucine zipper interaction with A kinase-anchoring protein 15

1 reference

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Characterization of Recombinant Skeletal Muscle (Ser-2843) and Cardiac Muscle (Ser-2809) Ryanodine Receptor Phosphorylation Mutants

1 reference

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Phospholamban: a crucial regulator of cardiac contractility

1 reference

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Transgenic CaMKIIdeltaC overexpression uniquely alters cardiac myocyte Ca2+ handling: reduced SR Ca2+ load and activated SR Ca2+ release

1 reference

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Intracellular targeting of protein kinases and phosphatases

2 references

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30 May 2018

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Targeting of alpha-kinase-anchoring protein (alpha KAP) to sarcoplasmic reticulum and nuclei of skeletal muscle.

1 reference

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Neuronal CA2+/calmodulin-dependent protein kinase II: the role of structure and autoregulation in cellular function

1 reference

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mAKAP and the ryanodine receptor are part of a multi-component signaling complex on the cardiomyocyte nuclear envelope

1 reference

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alphaKAP is an anchoring protein for a novel CaM kinase II isoform in skeletal muscle.

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The use of confocal microscopy in the investigation of cell structure and function in the heart, vascular endothelium and smooth muscle cells

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An alternative, nonkinase product of the brain-specifically expressed Ca2+/calmodulin-dependent kinase II alpha isoform gene in skeletal muscle

1 reference

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Alternative splicing introduces a nuclear localization signal that targets multifunctional CaM kinase to the nucleus

1 reference

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Isolation of the calmodulin-dependent protein kinase system from rabbit skeletal muscle sarcoplasmic reticulum

1 reference

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Two Ca2+ ATPase genes: homologies and mechanistic implications of deduced amino acid sequences

1 reference

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Phospholamban phosphorylation in intact ventricles. Phosphorylation of serine 16 and threonine 17 in response to beta-adrenergic stimulation

1 reference

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CaMKIIdelta isoforms differentially affect calcium handling but similarly regulate HDAC/MEF2 transcriptional responses

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Ouabain decreases sarco(endo)plasmic reticulum calcium ATPase activity in rat hearts by a process involving protein oxidation.

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The muscle-specific calmodulin-dependent protein kinase assembles with the glycolytic enzyme complex at the sarcoplasmic reticulum and modulates the activity of glyceraldehyde-3-phosphate dehydrogenase in a Ca2+/calmodulin-dependent manner

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Mechanism of enhanced cardiac function in mice with hypertrophy induced by overexpressed Akt.

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Identification of domains essential for the assembly of calcium/calmodulin-dependent protein kinase II holoenzymes

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A calmodulin-dependent protein kinase system from skeletal muscle sarcoplasmic reticulum

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Does Ca2+/calmodulin-dependent protein kinase deltac activate or inhibit the cardiac ryanodine receptor ion channel?

1 reference

https://pubmed.ncbi.nlm.nih.gov/19671701

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

1 reference

https://pubmed.ncbi.nlm.nih.gov/19671701

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

10.1074/JBC.M109.044990

1 reference

Europe PubMed Central

PMC publication ID

16 October 2017

PMC publication ID

1 reference

Europe PubMed Central

PMC publication ID

16 October 2017

PubMed publication ID

1 reference

Europe PubMed Central

PMC publication ID

16 October 2017

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