ArticleCirculation research2019
SPEG Controls Calcium Reuptake Into the Sarcoplasmic Reticulum Through Regulating SERCA2a by Its Second Kinase-Domain.
Article in Circulation research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 41 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
41 citing papers in PubMed, 55 citations in OpenAlex.
- Global adaptation to climate change in the twilight zone revealed by shared signals of selection in mesopelagic lanternfishes.bioRxiv : the preprint server for biology · 2026Article
- Calcium dysregulation in diabetic cardiomyopathy & heart failure with preserved ejection fraction.Frontiers in cardiovascular medicine · 2026Review
- The pathophysiological role of MiRNAs in heart failure.Frontiers in cardiovascular medicine · 2026Review
- Calcium handling remodeling in dilated cardiomyopathy: From molecular mechanisms to targeted therapies.Channels (Austin, Tex.) · 2025Review
- Phosphorylation of RYR1 at SerScience signaling · 2025Article
- Electrophysiological Mechanisms and Therapeutic Potential of Calcium Channels in Atrial Fibrillation.Reviews in cardiovascular medicine · 2025Review
- The varied functions of the giant muscle scaffold protein obscurin.Frontiers in cell and developmental biology · 2025Review
- AS160 is a lipid-responsive regulator of cardiac CaNature communications · 2024Article
- Lower diastolic tension may be indicative of higher proarrhythmic propensity in failing human cardiomyocytes.Scientific reports · 2024Article
- Integrated multi-omics approach reveals the role of striated muscle preferentially expressed protein kinase in skeletal muscle including its relationship with myospryn complex.Journal of cachexia, sarcopenia and muscle · 2024Article
- Speg interactions that regulate the stability of excitation-contraction coupling protein complexes in triads and dyads.Communications biology · 2023Article
- Novel SPEG variants in a neonate with severe dilated cardiomyopathy and relatively mild hypotonia.Human genome variation · 2023Article
- Translocation of IGF-1R in endoplasmic reticulum enhances SERCA2 activity to trigger CaActa pharmaceutica Sinica. B · 2023Article
- SERCA2 phosphorylation at serine 663 is a key regulator of CaNature communications · 2023Article
- Reduction in Junctophilin 2 Expression in Cardiac Nodal Tissue Results in Intracellular Calcium-Driven Increase in Nodal Cell Automaticity.Circulation. Arrhythmia and electrophysiology · 2023Article
- Dynamin-2 reduction rescues the skeletal myopathy of a SPEG-deficient mouse model.JCI insight · 2022Article
- A CaLife metabolism · 2022Article
- Impaired SERCA2a phosphorylation causes diabetic cardiomyopathy through impinging on cardiac contractility and precursor protein processing.Life metabolism · 2022Article
- The RalGAPα1-RalA signal module protects cardiac function through regulating calcium homeostasis.Nature communications · 2022Article
- Pyruvate Kinase M2 Protects Heart from Pressure Overload-Induced Heart Failure by Phosphorylating RAC1.Journal of the American Heart Association · 2022Article
Corrections and comments
- Commented on by
- Erratum issued
Authors and funding
13 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
rationaleSPEG (Striated muscle preferentially expressed protein kinase) has 2 kinase-domains and is critical for cardiac development and function. However, it is not clear how these 2 kinase-domains function to maintain cardiac performance.
objectiveTo determine the molecular functions of the 2 kinase-domains of SPEG. METHODS AND
resultsA proteomics approach identified SERCA2a (sarcoplasmic/endoplasmic reticulum calcium ATPase 2a) as a protein interacting with the second kinase-domain but not the first kinase-domain of SPEG. Furthermore, the second kinase-domain of SPEG could phosphorylate Thr
conclusionsOur data demonstrate that the 2 kinase-domains of SPEG may play distinct roles to regulate cardiac function. The second kinase-domain of SPEG is a critical regulator for SERCA2a. Our findings suggest that SPEG may serve as a new target to modulate SERCA2a activation for treatment of heart diseases with impaired calcium homeostasis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.