ArticleBiophysical journal2001
Locating phospholamban in co-crystals with Ca(2+)-ATPase by cryoelectron microscopy.
Article in Biophysical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 59 citations in OpenAlex.
- Sarcolipin is a Conformation-Dependent Regulator of the Sarcoplasmic Reticulum Calcium Pump SERCA.The Journal of membrane biology · 2026Article
- Distinct transport cycle and lipid regulation of a MgResearch square · 2026Article
- Structural Elements of Dwarf Open Reading Frame Required for Activation of the Sarco-Endoplasmic Reticulum Calcium Pump.Biochemistry · 2025Article
- Primitive Phospholamban- and Sarcolipin-like Peptides Inhibit the Sarcoplasmic Reticulum Calcium Pump SERCA.Biochemistry · 2022Article
- Alcohol Use Disorders and Their Harmful Effects on the Contractility of Skeletal, Cardiac and Smooth Muscles.Advances in drug and alcohol research · 2021Article
- Dwarf open reading frame (DWORF) is a direct activator of the sarcoplasmic reticulum calcium pump SERCA.eLife · 2021Article
- Atomistic Structure and Dynamics of the CaInternational journal of molecular sciences · 2020Article
- Interaction of a Sarcolipin Pentamer and Monomer with the Sarcoplasmic Reticulum Calcium Pump, SERCA.Biophysical journal · 2020Article
- The Phospholamban Pentamer Alters Function of the Sarcoplasmic Reticulum Calcium Pump SERCA.Biophysical journal · 2019Article
- Conformational memory in the association of the transmembrane protein phospholamban with the sarcoplasmic reticulum calcium pump SERCA.The Journal of biological chemistry · 2017Article
- Cardiac Calcium ATPase Dimerization Measured by Cross-Linking and Fluorescence Energy Transfer.Biophysical journal · 2016Article
- Regulation of the sarcoplasmic reticulum calcium pump by divergent phospholamban isoforms in zebrafish.The Journal of biological chemistry · 2015Article
- Phospholamban C-terminal residues are critical determinants of the structure and function of the calcium ATPase regulatory complex.The Journal of biological chemistry · 2014Article
- The FRET signatures of noninteracting proteins in membranes: simulations and experiments.Biophysical journal · 2014Article
- Allosteric regulation of SERCA by phosphorylation-mediated conformational shift of phospholamban.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Phosphorylated phospholamban stabilizes a compact conformation of the cardiac calcium-ATPase.Biophysical journal · 2013Article
- Sarco(endo)plasmic reticulum calcium ATPase (SERCA) inhibition by sarcolipin is encoded in its luminal tail.The Journal of biological chemistry · 2013Article
- Article
- Lethal, hereditary mutants of phospholamban elude phosphorylation by protein kinase A.The Journal of biological chemistry · 2012Article
- Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathy.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Phospholamban (PLB) is responsible for regulating Ca(2+) transport by Ca(2+)-ATPase across the sarcoplasmic reticulum of cardiac and smooth muscle. This regulation is coupled to beta-adrenergic stimulation, and dysfunction has been associated with end-stage heart failure. PLB appears to directly bind to Ca(2+)-ATPase, thus slowing certain steps in the Ca(2+) transport cycle. We have determined 3D structures from co-crystals of PLB with Ca(2+)-ATPase by cryoelectron microscopy of tubular co-crystals at 8--10 A resolution. Specifically, we have used wild-type PLB, a monomeric PLB mutant (L37A), and a pentameric PLB mutant (N27A) for co-reconstitution and have compared resulting structures with three control structures of Ca(2+)-ATPase alone. The overall molecular shape of Ca(2+)-ATPase was indistinguishable in the various reconstructions, indicating that PLB did not have any global effects on Ca(2+)-ATPase conformation. Difference maps reveal densities which we attributed to the cytoplasmic domain of PLB, though no difference densities were seen for PLB's transmembrane helix. Based on these difference maps, we propose that a single PLB molecule interacts with two Ca(2+)-ATPase molecules. Our model suggests that PLB may resist the large domain movements associated with the catalytic cycle, thus inhibiting turnover.
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