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Phospholamban

Phospholamban, Phospholemman, FXYD1
The protein encoded by this gene is found as a pentamer and is a major substrate for the cAMP-dependent protein kinase in cardiac muscle. The encoded protein is an inhibitor of cardiac muscle sarcoplasmic reticulum Ca(2+)-ATPase in the unphosphorylated state, but inhibition is relieved upon phosphorylation of the protein. The subsequent activation of the Ca(2+) pump leads to enhanced muscle relaxation rates, thereby contributing to the inotropic response elicited in heart by beta-agonists. The encoded protein is a key regulator of cardiac diastolic function. Mutations in this gene are a cause of inherited human dilated cardiomyopathy with refractory congestive heart failure. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ATPase, HAD, ACID, CAN, Alpha-1
Papers on Phospholamban
Muscle variables of importance for physiological performance in competitive football.
New
Nybo et al., Tórshavn, Faroe Islands. In Eur J Appl Physiol, Feb 2016
Peak 5-min game distance faster than 21 km h(-1) was related to the Na(+)-K(+) ATPase subunit (α1, α2, β1 and FXYD1) protein levels (r = 0.54-0.70),
Phospholamban spontaneously reconstitutes into giant unilamellar vesicles where it generates a cation selective channel.
New
Montis et al., Florence, Italy. In Phys Chem Chem Phys, Feb 2016
Phospholamban (PLN) is a small integral membrane protein, which modulates the activity of the Sarcoplasmic Reticulum Ca(2+)-ATPase (SERCA) of cardiac myocytes.
FXYD1 negatively regulates Na(+)/K(+)-ATPase activity in lung alveolar epithelial cells.
New
Morty et al., Gießen, Germany. In Respir Physiol Neurobiol, Jan 2016
We describe here increased expression of FXYD1, FXYD3 and FXYD5, three regulatory subunits of the Na(+)/K(+)-ATPase, in the lungs of ARDS patients.
Phospholamban and sarcolipin: Are they functionally redundant or distinct regulators of the Sarco(Endo)Plasmic Reticulum Calcium ATPase?
Review
New
Periasamy et al., Orlando, United States. In J Mol Cell Cardiol, Jan 2016
UNASSIGNED: In muscle, the Sarco(Endo)plasmic Reticulum Calcium ATPase (SERCA) activity is regulated by two distinct proteins, PLB and SLN, which are highly conserved throughout vertebrate evolution.
Phospholamban ablation rescues the enhanced propensity to arrhythmias of mice with CaMKII-constitutive phosphorylation of RyR2-S2814 site.
New
Mattiazzi et al., La Plata, Argentina. In J Physiol, Jan 2016
METHODS AND RESULTS: We generated PLN-deficient/S2814D(+/+) knock-in mice by crossing the two colonies (SD(+/+) /KO mice).
Phospholemman is not required for the acute stimulation of Na+-K+-ATPase α2-activity during skeletal muscle fatigue.
New
Heiny et al., Cincinnati, United States. In Am J Physiol Cell Physiol, Jan 2016
This study examines whether phosphorylation of phospholemman (PLM/FXYD1), a regulatory subunit of Na(+)-K(+)-ATPase, plays a role in the acute stimulation of α2 in working muscles.
Protein Phosphatase 1c Associated with the Cardiac Sodium Calcium Exchanger1 Regulates its Activity by Dephosphorylating Serine 68 Phosphorylated Phospholemman.
New
Carlson et al., Oslo, Norway. In J Biol Chem, Jan 2016
Serine 68 phosphorylated phospholemman (pSer-68-PLM) inhibits NCX1 activity.
Molecular Mechanisms and Kinetic Effects of FXYD1 and Phosphomimetic Mutants on Purified Human Na,K-ATPase.
New
Karlish et al., Konstanz, Germany. In J Biol Chem, Dec 2015
Phospholemman (FXYD1) is a single-transmembrane protein regulator of Na,K-ATPase, expressed strongly in heart, skeletal muscle, and brain and phosphorylated by protein kinases A and C at Ser-68 and Ser-63, respectively.
Importance of the Voltage Dependence of Cardiac Na/K ATPase Isozymes.
New
Artigas et al., San Juan, Puerto Rico. In Biophys J, Dec 2015
Furthermore, phospholemman (FXYD1) inhibits pump function without significantly altering the pump's voltage dependence.
Impact of phosphomimetic and non-phosphorylatable mutations of phospholemman on L-type calcium channels gating in HEK 293T cells.
New
Li et al., Shanghai, China. In J Cell Mol Med, Mar 2015
BACKGROUND: Phospholemman (PLM) is an important phosphorylation substrate for protein kinases A and C in the heart.
Novel regulation of cardiac Na pump via phospholemman.
Review
Shattock et al., London, United Kingdom. In J Mol Cell Cardiol, 2013
It is now widely recognized that phospholemman, a 72 amino acid accessory protein which forms part of the Na pump complex, is the key nexus linking cellular signaling to pump regulation.
Regulation of the cardiac sodium pump.
Review
Wypijewski et al., Dundee, United Kingdom. In Cell Mol Life Sci, 2013
The 72-residue phosphoprotein phospholemman regulates the sodium pump in the heart: unphosphorylated phospholemman inhibits the pump, and phospholemman phosphorylation increases pump activity.
Coordinated regulation of cardiac Na(+)/Ca (2+) exchanger and Na (+)-K (+)-ATPase by phospholemman (FXYD1).
Review
Wang et al., Philadelphia, United States. In Adv Exp Med Biol, 2012
Phospholemman (PLM) is the founding member of the FXYD family of regulators of ion transport.
Intracellular trafficking of FXYD1 (phospholemman) and FXYD7 proteins in Xenopus oocytes and mammalian cells.
GeneRIF
Garty et al., Israel. In J Biol Chem, 2012
Intracellular trafficking of FXYD1 (phospholemman) and FXYD7 proteins in Xenopus oocytes and mammalian cells.
Phospholemman deficiency in postinfarct hearts: enhanced contractility but increased mortality.
GeneRIF
Tucker et al., Charlottesville, United States. In Clin Transl Sci, 2012
Alterations in PLM expression and phosphorylation are important adaptations post-myocardial infarction.
Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathy.
GeneRIF
Young et al., Edmonton, Canada. In J Biol Chem, 2012
Hydrophobic imbalance in the cytoplasmic domain of phospholamban is a determinant for lethal dilated cardiomyopathy.
Phospholamban and cardiac function: a comparative perspective in vertebrates.
Review
Imbrogno et al., Rende, Italy. In Acta Physiol (oxf), 2012
Phospholamban (PLN) is a small phosphoprotein closely associated with the cardiac sarcoplasmic reticulum (SR).
Influence of chronic and acute spinal cord injury on skeletal muscle Na+-K+-ATPase and phospholemman expression in humans.
GeneRIF
Chibalin et al., Stockholm, Sweden. In Am J Physiol Endocrinol Metab, 2012
the severity of the spinal cord lesion is an important factor controlling the expression of Na(+)-K(+)-ATPase and its regulatory protein PLM
Chronic nicotine modifies skeletal muscle Na,K-ATPase activity through its interaction with the nicotinic acetylcholine receptor and phospholemman.
GeneRIF
Krivoi et al., Stockholm, Sweden. In Plos One, 2011
Chronic nicotine modifies skeletal muscle Na,K-ATPase activity through its interaction with the nicotinic acetylcholine receptor and phospholemman.
Unitary anion currents through phospholemman channel molecules.
Impact
Jones et al., Charlottesville, United States. In Nature, 1995
Phospholemman (PLM) is a 72-amino-acid peptide with a single transmembrane domain, the expression of which induces chloride currents in Xenopus oocytes.
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