ArticleProtein science : a publication of the Protein Society2006
Secondary structure, orientation, and oligomerization of phospholemman, a cardiac transmembrane protein.
Article in Protein science : a publication of the Protein Society, 2006. 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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27 citing papers in PubMed, 49 citations in OpenAlex.
- Structure and Function of Canine SP-C Mimic Proteins in Synthetic Surfactant Lipid Dispersions.Biomedicines · 2024Article
- 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
- L30A Mutation of Phospholemman Mimics Effects of Cardiac Glycosides in Isolated Cardiomyocytes.Biochemistry · 2016Article
- Na+/Ca2+ exchange and Na+/K+-ATPase in the heart.The Journal of physiology · 2015Review
- Article
- 2D IR cross peaks reveal hydrogen-deuterium exchange with single residue specificity.The journal of physical chemistry. B · 2013Article
- Site-specific orientation of an α-helical peptide ovispirin-1 from isotope-labeled SFG spectroscopy.The journal of physical chemistry. B · 2013Article
- 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
- Phosphomimetic mutations enhance oligomerization of phospholemman and modulate its interaction with the Na/K-ATPase.The Journal of biological chemistry · 2011Article
- Phospholemman: a novel cardiac stress protein.Clinical and translational science · 2010Review
- Orientation and dynamics of transmembrane peptides: the power of simple models.European biophysics journal : EBJ · 2010Review
- Isoform specificity of the Na/K-ATPase association and regulation by phospholemman.The Journal of biological chemistry · 2009Article
- Interaction and conformational dynamics of membrane-spanning protein helices.Protein science : a publication of the Protein Society · 2009Review
- Na/K-ATPase--an integral player in the adrenergic fight-or-flight response.Trends in cardiovascular medicine · 2009Review
- Phospholemman regulates cardiac Na+/Ca2+ exchanger by interacting with the exchanger's proximal linker domain.American journal of physiology. Cell physiology · 2009Article
- The strong dimerization of the transmembrane domain of the fibroblast growth factor receptor (FGFR) is modulated by C-terminal juxtamembrane residues.Protein science : a publication of the Protein Society · 2009Article
- Structural flexibility of the pentameric SARS coronavirus envelope protein ion channel.Biophysical journal · 2008Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human phospholemman (PLM) is a 72-residue protein, which is expressed at high density in the cardiac plasma membrane and in various other tissues. It forms ion channels selective for K+, Cl-, and taurine in lipid bilayers and colocalizes with the Na+/K+-ATPase and the Na+/Ca2+-exchanger, which may suggest a role in the regulation of cell volume. Here we present the first structural data based on synthetic peptides representing the transmembrane domain of PLM. Perfluoro-octaneoate-PAGE of reconstituted proteoliposomes containing PLM reveals a tetrameric homo-oligomerization. Infrared spectroscopy of proteoliposomes shows that the PLM peptide is completely alpha-helical, even beyond the hydrophobic core residues. Hydrogen/deuterium exchange experiments reveal that a core of 20-22 residues is not accessible to water, thus embedded in the lipid membrane. The maximum helix tilt is 17 degrees +/- 2 degrees obtained by attenuated total reflection infrared spectroscopy. Thus, our data support the idea of ion channel formation by the PLM transmembrane domain.
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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.