ArticleThe Journal of biological chemistry2015
The N Terminus of Sarcolipin Plays an Important Role in Uncoupling Sarco-endoplasmic Reticulum Ca2+-ATPase (SERCA) ATP Hydrolysis from Ca2+ Transport.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 63 citations in OpenAlex.
- Sarcolipin is a Conformation-Dependent Regulator of the Sarcoplasmic Reticulum Calcium Pump SERCA.The Journal of membrane biology · 2026Article
- The Pathogenesis of Preeclampsia: Hypoxia and the Unfolded Protein Response.Reproductive sciences (Thousand Oaks, Calif.) · 2026Review
- Effects of electromyostimulation on sarcolipin and CaBiochemistry and biophysics reports · 2026Article
- Impact of sarcopenia and obesity on skeletal muscle size, gene expression, and mitochondrial function.GeroScience · 2026Article
- Dual-Targeted Glucose-Dependent Insulinotropic Polypeptide-Loaded Photothermal Nanoparticles to Prevent Obesity via Lipolysis and Browning of White Adipose Tissue.Small science · 2025Article
- Molecular mechanisms of UCP1-independent thermogenesis: the role of futile cycles in energy dissipation.Journal of physiology and biochemistry · 2025Review
- The GIP receptor activates futile calcium cycling in white adipose tissue to increase energy expenditure and drive weight loss in mice.Cell metabolism · 2025Article
- Article
- Hypermetabolism in mice carrying a near complete human chromosome 21.bioRxiv : the preprint server for biology · 2023Article
- Recruitment of Muscle Genes as an Effect of Brown Adipose Tissue Ablation in Cold-Acclimated Brandt's Voles (International journal of molecular sciences · 2022Article
- Knockdown of sarcolipin (SLN) impairs substrate utilization in human skeletal muscle cells.Molecular biology reports · 2022Article
- Calcium cycling as a mediator of thermogenic metabolism in adipose tissue.Molecular pharmacology · 2022Article
- Whole-body endothermy: ancient, homologous and widespread among the ancestors of mammals, birds and crocodylians.Biological reviews of the Cambridge Philosophical Society · 2022Article
- Structural basis for sarcolipin's regulation of muscle thermogenesis by the sarcoplasmic reticulum CaScience advances · 2021Article
- Sarcoplasmic Reticulum from Horse Gluteal Muscle Is Poised for Enhanced Calcium Transport.Veterinary sciences · 2021Article
- Strain-specific differences in muscle CaThe Journal of experimental biology · 2021Article
- Is Upregulation of Sarcolipin Beneficial or Detrimental to Muscle Function?Frontiers in physiology · 2021Article
- Sarcolipin Exhibits Abundant RNA Transcription and Minimal Protein Expression in Horse Gluteal Muscle.Veterinary sciences · 2020Article
- Neuronatin regulates whole-body metabolism: is thermogenesis involved?FASEB bioAdvances · 2020Article
- Conserved Luminal C-Terminal Domain Dynamically Controls Interdomain Communication in Sarcolipin.Journal of chemical information and modeling · 2020Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
The sarcoendoplasmic reticulum Ca(2+)-ATPase (SERCA) is responsible for intracellular Ca(2+) homeostasis. SERCA activity in muscle can be regulated by phospholamban (PLB), an affinity modulator, and sarcolipin (SLN), an uncoupler. Although PLB gets dislodged from Ca(2+)-bound SERCA, SLN continues to bind SERCA throughout its kinetic cycle and promotes uncoupling of Ca(2+) transport from ATP hydrolysis. To determine the structural regions of SLN that mediate uncoupling of SERCA, we employed mutagenesis and generated chimeras of PLB and SLN. In this study we demonstrate that deletion of SLN N-terminal residues (2)ERSTQ leads to loss of the uncoupling function even though the truncated peptide can target and constitutively bind SERCA. Furthermore, molecular dynamics simulations of SLN and SERCA interaction showed a rearrangement of SERCA residues that is altered when the SLN N terminus is deleted. Interestingly, transfer of the PLB cytosolic domain to the SLN transmembrane (TM) and luminal tail causes the chimeric protein to lose SLN-like function. Further introduction of the PLB TM region into this chimera resulted in conversion to full PLB-like function. We also found that swapping PLB N and C termini with those from SLN caused the resulting chimera to acquire SLN-like function. Swapping the C terminus alone was not sufficient for this conversion. These results suggest that domains can be switched between SLN and PLB without losing the ability to regulate SERCA activity; however, the resulting chimeras acquire functions different from the parent molecules. Importantly, our studies highlight that the N termini of SLN and PLB influence their respective unique functions.
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