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FXYD1 encodes a member of a family of small membrane proteins that share a 35-amino acid signature sequence domain, beginning with the sequence PFXYD and containing 7 invariant and 6 highly conserved amino acids. Additionally we are shipping FXYD1 Antibodies (96) and FXYD1 Proteins (3) and many more products for this protein.
Study demonstrated that the expression of FXYD1, FXYD3 (show FXYD3 ELISA Kits) and FXYD5 (show FXYD5 ELISA Kits) is elevated in the lungs of Acute respiratory distress syndrome patients
a period of high-intensity training with reduced training volume increases expression and phosphorylation levels of FXYD1, which may affect Na(+)/K(+) pump activity and muscle K(+) homeostasis during intense exercise.
Stopped-flow experiments using the dye RH421 show that FXYD1 slows the conformational transition E2(2K)ATP --> E1(3Na)ATP but does not affect 3NaE1P --> E2P3Na.
the evolutionary conservation of G-quadruplex forming sequences with the confirmation of G-quadruplex formation in vitro by two FXYD1 homologues
Phospholemman is the target of a variety of post-translational modifications and these can dynamically alter the activity of the Na pump. [Review]
PLM regulates important ion transporters in the heart and offers a tempting target for development of drugs to treat heart failure.
Intracellular trafficking of FXYD1 (phospholemman) and FXYD7 (show FXYD7 ELISA Kits) proteins in Xenopus oocytes and mammalian cells.
the severity of the spinal cord lesion is an important factor controlling the expression of Na(+)-K(+)-ATPase (show ATP1A1 ELISA Kits) and its regulatory protein PLM
in left ventricular myocardium from patients with heart failure, PLM Ser (show SIGLEC1 ELISA Kits)-68 phosphorylation was approximately 50% lower than in nonfailing controls
Exercise induces FXYD1 phosphorylation at multiple sites in human muscle; in mice, contraction-induced changes in FXYD1 phosphorylation are fiber-type specific and dependent on protein kinase (show CDK7 ELISA Kits) Calpha (show PRKACA ELISA Kits) activity.
S68 phospholemman phosphorylation may be involved in cAMP-dependent regulation of smooth muscle force.
Phospholemman does not participate in forskolin-induced swine carotid artery relaxation.
Both the extracellular PFXYD motif and the transmembrane domain of PLM but not the cytoplasmic tail were necessary for regulation of peak L-type Ca(2 (show CA2 ELISA Kits)+) current amplitude.
Decreased phosphorylation of PLM reduces Na/K pump activity and exacerbates Na overload, contractile dysfunction, and adverse remodelling following aortic constriction in mice.
Nitric oxide activates Na/K-ATPase (show ATP1A1 ELISA Kits) via phospholemman phosphorylation.
The results of this study indicated that reducing FXYD1 levels improves a specific cognitive impairment in MECP2-deficient mice.
Alterations in PLM expression and phosphorylation are important adaptations post-myocardial infarction.
The results of this study showed the involvement of epigenetic mechanisms in the manifestation of brain region-specific differences in Fxyd1 expression.
Under catecholamine stress when [Na+]i is high, phospholemman minimizes [Na+]i overload by relieving its inhibition of Na+-K+-ATPase (show ATP1A1 ELISA Kits) and preserves inotropy by simultaneously inhibiting Na+/Ca2+ exchanger (show SLC8A1 ELISA Kits).
Under stressful conditions in which [Na(+)](i) was high, beta-adrenergic agonist-mediated phosphorylation of phospholemman resulted in time-dependent reduction in inotropy due to relief of inhibition of Na(+)-K(+)-ATPase (show ATP1A1 ELISA Kits).
a primary effect of phospholemman is to modulate the Na-K-ATPase (show ATP1A1 ELISA Kits) and that its reduced activity initiates compensatory responses in heart hypertrophy
This gene encodes a member of a family of small membrane proteins that share a 35-amino acid signature sequence domain, beginning with the sequence PFXYD and containing 7 invariant and 6 highly conserved amino acids. The approved human gene nomenclature for the family is FXYD-domain containing ion transport regulator. Mouse FXYD5 has been termed RIC (Related to Ion Channel). FXYD2, also known as the gamma subunit of the Na,K-ATPase, regulates the properties of that enzyme. FXYD1 (phospholemman), FXYD2 (gamma), FXYD3 (MAT-8), FXYD4 (CHIF), and FXYD5 (RIC) have been shown to induce channel activity in experimental expression systems. Transmembrane topology has been established for two family members (FXYD1 and FXYD2), with the N-terminus extracellular and the C-terminus on the cytoplasmic side of the membrane. The protein encoded by this gene is a plasma membrane substrate for several kinases, including protein kinase A, protein kinase C, NIMA kinase, and myotonic dystrophy kinase. It is thought to form an ion channel or regulate ion channel activity. Transcript variants with different 5' UTR sequences have been described in the literature.
FXYD domain containing ion transport regulator 1
, FXYD domain containing ion transport regulator 1 (phospholemman)
, FXYD domain-containing ion transport regulator 1