ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structural topology of phospholamban pentamer in lipid bilayers by a hybrid solution and solid-state NMR method.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.
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Who cites it
102 citing papers in PubMed, 172 citations in OpenAlex.
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- Dipolar Recoupling in Rotating Solids.Chemical reviews · 2024Review
- Analysis of the structure and interactions of the SARS-CoV-2 ORF7b accessory protein.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Pathological mutations in the phospholamban cytoplasmic region affect its topology and dynamics modulating the extent of SERCA inhibition.Biochimica et biophysica acta. Biomembranes · 2024Article
- Phosphorylation of phospholamban promotes SERCA2a activation by dwarf open reading frame (DWORF).Cell calcium · 2024Article
- Phospholamban pentamerization increases sensitivity and dynamic range of cardiac relaxation.Cardiovascular research · 2023Article
- Protein Design: From the Aspect of Water Solubility and Stability.Chemical reviews · 2022Review
- A kink in DWORF helical structure controls the activation of the sarcoplasmic reticulum CaStructure (London, England : 1993) · 2022Article
- Homologous cardiac calcium pump regulators phospholamban and sarcolipin adopt distinct oligomeric states in the membrane.Computational and structural biotechnology journal · 2022Article
- Towards a native environment: structure and function of membrane proteins in lipid bilayers by NMR.Chemical science · 2021Review
- Nothing Regular about the Regulins: Distinct Functional Properties of SERCA Transmembrane Peptide Regulatory Subunits.International journal of molecular sciences · 2021Review
- Molecular noise filtering in the β-adrenergic signaling network by phospholamban pentamers.Cell reports · 2021Article
- Dwarf open reading frame (DWORF) is a direct activator of the sarcoplasmic reticulum calcium pump SERCA.eLife · 2021Article
- Structural basis for allosteric control of the SERCA-Phospholamban membrane complex by CaeLife · 2021Article
- Solid-State NMR of Membrane Proteins in Lipid Bilayers: To Spin or Not To Spin?Accounts of chemical research · 2021Review
- Interaction of a Sarcolipin Pentamer and Monomer with the Sarcoplasmic Reticulum Calcium Pump, SERCA.Biophysical journal · 2020Article
- A theoretical assessment of structure determination of multi-span membrane proteins by oriented sample solid-state NMR spectroscopy.Australian journal of chemistry · 2020Article
- Newly Discovered Micropeptide Regulators of SERCA Form Oligomers but Bind to the Pump as Monomers.Journal of molecular biology · 2019Article
- Solution NMR: A powerful tool for structural and functional studies of membrane proteins in reconstituted environments.The Journal of biological chemistry · 2019Review
- Breaking the Backbone: Central Arginine Residues Induce Membrane Exit and Helix Distortions within a Dynamic Membrane Peptide.The journal of physical chemistry. B · 2019Article
42 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Phospholamban (PLN) is a type II membrane protein that inhibits the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA), thereby regulating calcium homeostasis in cardiac muscle. In membranes, PLN forms pentamers that have been proposed to function either as a storage for active monomers or as ion channels. Here, we report the T-state structure of pentameric PLN solved by a hybrid solution and solid-state NMR method. In lipid bilayers, PLN adopts a pinwheel topology with a narrow hydrophobic pore, which excludes ion transport. In the T state, the cytoplasmic amphipathic helices (domains Ia) are absorbed into the lipid bilayer with the transmembrane domains arranged in a left-handed coiled-coil configuration, crossing the bilayer with a tilt angle of approximately 11° with respect to the membrane normal. The tilt angle difference between the monomer and pentamer is approximately 13°, showing that intramembrane helix-helix association forces dominate over the hydrophobic mismatch, driving the overall topology of the transmembrane assembly. Our data reveal that both topology and function of PLN are shaped by the interactions with lipids, which fine-tune the regulation of SERCA.
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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.