ArticleBiophysical journal2012
Protein-protein interactions in calcium transport regulation probed by saturation transfer electron paramagnetic resonance.
Article in Biophysical journal, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 41 citations in OpenAlex.
- A high-sensitivity stopped-flow EPR system to monitor millisecond conformational kinetics in spin-labeled proteins.Protein science : a publication of the Protein Society · 2025Article
- Capturing protein dynamics across timescales with site-directed spin labeling electron paramagnetic resonance spectroscopy.Current opinion in structural biology · 2025Review
- A Highly Ordered Nitroxide Side Chain for Distance Mapping and Monitoring Slow Structural Fluctuations in Proteins.Applied magnetic resonance · 2024Article
- Protein Crowding and Cholesterol Increase Cell Membrane Viscosity in a Temperature Dependent Manner.Journal of chemical theory and computation · 2023Article
- Interaction of DWORF with SERCA and PLB as determined by EPR spectroscopy.Biochemical and biophysical research communications · 2023Article
- Structural basis for allosteric control of the SERCA-Phospholamban membrane complex by CaeLife · 2021Article
- Atomistic Structure and Dynamics of the CaInternational journal of molecular sciences · 2020Article
- Nitroxyl (HNO) targets phospholamban cysteines 41 and 46 to enhance cardiac function.The Journal of general physiology · 2019Article
- Influenza A M2 Channel Clustering at High Protein/Lipid Ratios: Viral Budding Implications.Biophysical journal · 2019Article
- The Phospholamban Pentamer Alters Function of the Sarcoplasmic Reticulum Calcium Pump SERCA.Biophysical journal · 2019Article
- Phospholamban regulates nuclear CaJournal of molecular and cellular cardiology · 2018Article
- Targeting protein-protein interactions for therapeutic discovery via FRET-based high-throughput screening in living cells.Scientific reports · 2018Article
- Structural basis for relief of phospholamban-mediated inhibition of the sarcoplasmic reticulum CaThe Journal of biological chemistry · 2018Article
- Effect of Phosphorylation on Interactions between Transmembrane Domains of SERCA and Phospholamban.Biophysical journal · 2018Article
- Slow Dynamics around a Protein and Its Coupling to Solvent.ACS central science · 2018Article
- Maleimido-proxyl as an EPR spin label for the evaluation of conformational changes of albumin.European biophysics journal : EBJ · 2017Article
- A bifunctional spin label reports the structural topology of phospholamban in magnetically-aligned bicelles.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2016Article
- Atomic-level mechanisms for phospholamban regulation of the calcium pump.Biophysical journal · 2015Article
- Phospholamban phosphorylation, mutation, and structural dynamics: a biophysical approach to understanding and treating cardiomyopathy.Biophysical reviews · 2015Article
- Optimization of bicelle lipid composition and temperature for EPR spectroscopy of aligned membranes.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2015Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
We have used electron paramagnetic resonance (EPR) to probe the homo- and heterooligomeric interactions of reconstituted sarcoplasmic reticulum Ca-ATPase (SERCA) and its regulator phospholamban (PLB). SERCA is responsible for restoring calcium to the sarcoplasmic reticulum to allow muscle relaxation, whereas PLB inhibits cardiac SERCA unless phosphorylated at Ser(16). To determine whether changes in protein association play essential roles in regulation, we detected the microsecond rotational diffusion of both proteins using saturation transfer EPR. Peptide synthesis was used to create a fully functional and monomeric PLB mutant with a spin label rigidly coupled to the backbone of the transmembrane helix, while SERCA was reacted with a Cys-specific spin label. Saturation transfer EPR revealed that sufficiently high lipid/protein ratios minimized self-association for both proteins. Under these dilute conditions, labeled PLB was substantially immobilized after co-reconstitution with unlabeled SERCA, reflecting their association to form the regulatory complex. Ser(16) phosphorylation slightly increased this immobilization. Complementary measurements with labeled SERCA showed no change in mobility after co-reconstitution with unlabeled PLB, regardless of its phosphorylation state. We conclude that phosphorylating monomeric PLB can relieve SERCA inhibition without changes in the oligomeric states of these proteins, indicating a structural rearrangement within the heterodimeric regulatory complex.
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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.