ArticleThe Journal of biological chemistry2011
Phosphomimetic mutations enhance oligomerization of phospholemman and modulate its interaction with the Na/K-ATPase.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Micropeptide hetero-oligomerization adds complexity to the calcium pump regulatory network.Biophysical journal · 2023Article
- Fluorescence lifetime imaging microscopy reveals sodium pump dimers in live cells.The Journal of biological chemistry · 2022Article
- FXYD proteins and sodium pump regulatory mechanisms.The Journal of general physiology · 2021Review
- Design of a Proteolytically Stable Sodium-Calcium Exchanger 1 Activator Peptide forFrontiers in pharmacology · 2021Article
- A unique bZIP transcription factor imparting multiple stress tolerance in Rice.Rice (New York, N.Y.) · 2019Article
- Impaired AQP2 trafficking in Fxyd1 knockout mice: A role for FXYD1 in regulated vesicular transport.PloS one · 2017Article
- L30A Mutation of Phospholemman Mimics Effects of Cardiac Glycosides in Isolated Cardiomyocytes.Biochemistry · 2016Article
- Cardiac Calcium ATPase Dimerization Measured by Cross-Linking and Fluorescence Energy Transfer.Biophysical journal · 2016Article
- Development of a high-affinity peptide that prevents phospholemman (PLM) inhibition of the sodium/calcium exchanger 1 (NCX1).The Biochemical journal · 2016Article
- ATP-Binding Cassette Transporter Structure Changes Detected by Intramolecular Fluorescence Energy Transfer for High-Throughput Screening.Molecular pharmacology · 2015Article
- Na+/Ca2+ exchange and Na+/K+-ATPase in the heart.The Journal of physiology · 2015Review
- A separate pool of cardiac phospholemman that does not regulate or associate with the sodium pump: multimers of phospholemman in ventricular muscle.The Journal of biological chemistry · 2013Article
- Regulation of the cardiac sodium pump.Cellular and molecular life sciences : CMLS · 2013Review
- Na⁺/K⁺-ATPase E960 and phospholemman F28 are critical for their functional interaction.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- 2-Color calcium pump reveals closure of the cytoplasmic headpiece with calcium binding.PloS one · 2012Article
- The inhibitory effect of phospholemman on the sodium pump requires its palmitoylation.The Journal of biological chemistry · 2011Article
- Phospholamban binds with differential affinity to calcium pump conformers.The Journal of biological chemistry · 2011Article
- Residues 248-252 and 300-304 of the cardiac Na+/Ca2+ exchanger are involved in its regulation by phospholemman.American journal of physiology. Cell physiology · 2011Article
- Oligomeric interactions of sarcolipin and the Ca-ATPase.The Journal of biological chemistry · 2011Article
- Evolutionary patterns of phosphorylated serines.Biology direct · 2011Article
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Na/K-ATPase (NKA) activity is dynamically regulated by an inhibitory interaction with a small transmembrane protein, phospholemman (PLM). Inhibition is relieved upon PLM phosphorylation. Phosphorylation may alter how PLM interacts with NKA and/or itself, but details of these interactions are unknown. To address this, we quantified FRET between PLM and its regulatory target NKA in live cells. Phosphorylation of PLM was mimicked by mutation S63E (PKC site), S68E (PKA/PKC site), or S63E/S68E. The dependence of FRET on protein expression in live cells yielded information about the structure and binding affinity of the PLM-NKA regulatory complex. PLM phosphomimetic mutations altered the quaternary structure of the regulatory complex and reduced the apparent affinity of the PLM-NKA interaction. The latter effect was likely due to increased oligomerization of PLM phosphomimetic mutants, as suggested by PLM-PLM FRET measurements. Distance constraints obtained by FRET suggest that phosphomimetic mutations slightly alter the oligomer quaternary conformation. Photon-counting histogram measurements revealed that the major PLM oligomeric species is a tetramer. We conclude that phosphorylation of PLM increases its oligomerization into tetramers, decreases its binding to NKA, and alters the structures of both the tetramer and NKA regulatory complex.
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