ArticleJournal of molecular biology2011
Phosphorylation and mutation of phospholamban alter physical interactions with the sarcoplasmic reticulum calcium pump.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 67 citations in OpenAlex.
- No Time to Fold: Intrinsically Disordered Microproteins in Action.Biochemistry · 2026Review
- Microprotein, macro-effect: DWORF as a therapeutic strategy in heart failure.Frontiers in cell and developmental biology · 2026Review
- Replacement of Lys27 by asparagine in the SERCA regulator myoregulin: A CaBiochimica et biophysica acta. Molecular cell research · 2024Review
- Phospholamban pentamerization increases sensitivity and dynamic range of cardiac relaxation.Cardiovascular research · 2023Article
- Functional Role of an Unusual Transmembrane Acidic Residue in the Calcium Pump Regulator Myoregulin.Biochemistry · 2023Article
- Primitive Phospholamban- and Sarcolipin-like Peptides Inhibit the Sarcoplasmic Reticulum Calcium Pump SERCA.Biochemistry · 2022Article
- Stimulation of CaChemMedChem · 2021Article
- Serum response factor deletion 5 regulates phospholamban phosphorylation and calcium uptake.Journal of molecular and cellular cardiology · 2021Article
- Nothing Regular about the Regulins: Distinct Functional Properties of SERCA Transmembrane Peptide Regulatory Subunits.International journal of molecular sciences · 2021Review
- Dynamics-Driven Allostery Underlies CaBiophysical journal · 2020Article
- Atomistic Structure and Dynamics of the CaInternational journal of molecular sciences · 2020Article
- Protein Adsorption on Solid Supported Membranes: Monitoring the Transport Activity of P-Type ATPases.Molecules (Basel, Switzerland) · 2020Review
- Protein docking and steered molecular dynamics suggest alternative phospholamban-binding sites on the SERCA calcium transporter.The Journal of biological chemistry · 2020Article
- Interaction of a Sarcolipin Pentamer and Monomer with the Sarcoplasmic Reticulum Calcium Pump, SERCA.Biophysical journal · 2020Article
- Tracking nitroxyl-derived posttranslational modifications of phospholamban in cardiac myocytes.The Journal of general physiology · 2019Article
- Nitroxyl (HNO) targets phospholamban cysteines 41 and 46 to enhance cardiac function.The Journal of general physiology · 2019Article
- Thermodynamics of Cation Binding to the Sarcoendoplasmic Reticulum Calcium ATPase Pump and Impacts on Enzyme Function.Journal of chemical theory and computation · 2019Article
- 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
- Disulfide-activated protein kinase G Iα regulates cardiac diastolic relaxation and fine-tunes the Frank-Starling response.Nature communications · 2016Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Phospholamban physically interacts with the sarcoplasmic reticulum calcium pump (SERCA) and regulates contractility of the heart in response to adrenergic stimuli. We studied this interaction using electron microscopy of 2D crystals of SERCA in complex with phospholamban. In earlier studies, phospholamban oligomers were found interspersed between SERCA dimer ribbons and a 3D model was constructed to show interactions with SERCA. In this study, we examined the oligomeric state of phospholamban and the effects of phosphorylation and mutation of phospholamban on the interaction with SERCA in the 2D crystals. On the basis of projection maps from negatively stained and frozen-hydrated crystals, phosphorylation of Ser16 selectively disordered the cytoplasmic domain of wild type phospholamban. This was not the case for a pentameric gain-of-function mutant (Lys27Ala), which retained inhibitory activity and remained ordered in the phosphorylated state. A partial loss-of-function mutation that altered the charge state of phospholamban (Arg14Ala) retained an ordered state, while a complete loss-of-function mutation (Asn34Ala) was also disordered. The functional state of phospholamban was correlated with an order-to-disorder transition of the phospholamban cytoplasmic domain in the 2D co-crystals. Furthermore, co-crystals of the gain-of-function mutant (Lys27Ala) facilitated data collection from frozen-hydrated crystals. An improved projection map was calculated to a resolution of 8 Å, which supports the pentamer as the oligomeric state of phospholamban in the crystals. The 2D co-crystals with SERCA require a functional pentameric form of phospholamban, which physically interacts with SERCA at an accessory site distinct from that used by the phospholamban monomer for the inhibitory association.
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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.