ArticleNature2013
The sarcolipin-bound calcium pump stabilizes calcium sites exposed to the cytoplasm.
Article in Nature, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
117 citing papers in PubMed, 212 citations in OpenAlex.
- Sarcolipin is a Conformation-Dependent Regulator of the Sarcoplasmic Reticulum Calcium Pump SERCA.The Journal of membrane biology · 2026Article
- Active conformations of neuronal NaNature communications · 2026Article
- Distinct transport cycle and lipid regulation of a MgResearch square · 2026Article
- Supercharging the calcium pump: Identification of an activation hotspot on SERCA by cryo-EM.bioRxiv : the preprint server for biology · 2026Article
- The Landscape of SERCA2 in Cardiovascular Diseases: Expression Regulation, Therapeutic Applications, and Emerging Roles.Biomolecules · 2026Review
- Sarcolipin-SERCA uncoupling as a plausible heat source for sustaining fever.Frontiers in physiology · 2026Article
- Article
- Endogenous structure of antimalarial target PfATP4 reveals an apicomplexan-specific P-type ATPase modulator.Nature communications · 2025Article
- Allosteric Modulation of SERCA Pumps in Health and Disease: Structural Dynamics, Posttranslational Modifications, and Therapeutic Potential.Journal of molecular biology · 2025Review
- Article
- P-type ATPase magnesium transporter MgtA acts as a dimer.Nature structural & molecular biology · 2025Article
- Identification of a molecular resistor that controls UCP1-independent CaCell metabolism · 2025Article
- Sarcoendoplasmic reticulum calcium ATPase is an essential and druggable lipid-dependent ion pump in Toxoplasma gondii.Communications biology · 2025Article
- S100A1ct: A Synthetic Peptide Derived From S100A1 Protein Improves Cardiac Performance and Survival in Preclinical Heart Failure Models.Circulation · 2025Article
- The structure and function of P5A-ATPases.Nature communications · 2024Article
- Dephosphorylation and ion binding in prokaryotic calcium transport.Science advances · 2024Article
- Diverse roles of the metal binding domains and transport mechanism of copper transporting P-type ATPases.Nature communications · 2024Article
- Replacement of Lys27 by asparagine in the SERCA regulator myoregulin: A CaBiochimica et biophysica acta. Molecular cell research · 2024Review
- Functional Role of an Unusual Transmembrane Acidic Residue in the Calcium Pump Regulator Myoregulin.Biochemistry · 2023Article
- The Meeting of Micropeptides with Major CaMembranes · 2023Review
57 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The contraction and relaxation of muscle cells is controlled by the successive rise and fall of cytosolic Ca(2+), initiated by the release of Ca(2+) from the sarcoplasmic reticulum and terminated by re-sequestration of Ca(2+) into the sarcoplasmic reticulum as the main mechanism of Ca(2+) removal. Re-sequestration requires active transport and is catalysed by the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA), which has a key role in defining the contractile properties of skeletal and heart muscle tissue. The activity of SERCA is regulated by two small, homologous membrane proteins called phospholamban (PLB, also known as PLN) and sarcolipin (SLN). Detailed structural information explaining this regulatory mechanism has been lacking, and the structural features defining the pathway through which cytoplasmic Ca(2+) enters the intramembranous binding sites of SERCA have remained unknown. Here we report the crystal structure of rabbit SERCA1a (also known as ATP2A1) in complex with SLN at 3.1 Å resolution. The regulatory SLN traps the Ca(2+)-ATPase in a previously undescribed E1 state, with exposure of the Ca(2+) sites through an open cytoplasmic pathway stabilized by Mg(2+). The structure suggests a mechanism for selective Ca(2+) loading and activation of SERCA, and provides new insight into how SLN and PLB inhibition arises from stabilization of this E1 intermediate state without bound Ca(2+). These findings may prove useful in studying how autoinhibitory domains of other ion pumps modulate transport across biological membranes.
Indexed as
Identifiers
What OpenQuestion holds
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.