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SLN overexpression is associated with severe muscle atrophy and weakness.
SLN plays an important role in adaptive muscle remodeling potentially through calcineurin stimulation, which could have important implications for other muscle diseases and conditions
Cardiac function of Sln(Cre/+) mice was not significantly different from WT mice in all aspects that were examined.
increased expression improves skeletal muscle performance during prolonged muscle activity by increasing store-operated calcium entry and muscle energetics
the N termini of SLN and PLB influence their respective unique functions
UCP1 and SLN are required to maintain optimal thermogenesis and loss of both systems compromises survival of mice under cold stress
both SLN knockout (Sln(-/-)) and skeletal muscle-specific SLN overexpression (Sln(OE)) mice to explore energy metabolism by pair feeding (fixed calories) and high-fat diet feeding (ad libitum)
overexpression of neither wild type nor FLAG-tagged variants of sarcolipin in transgenic mice had any major significant effects on body mass, energy expenditure, even when mice were fed on a high fat diet
SLN and PLN are co-expressed in most fibers, which suggests that super-inhibition of SERCAs may be physiologically important in the regulation of intracellular Ca2+ in human skeletal muscle.
results suggest that beta-AR signaling partially compensates for a lack of SLN to activate muscle-based DIT, but SLN is the primary and more effective mediator.
Sarcolipin deficiency increases the transport stoichiometry of SERCA pumps and decreases the relative contribution of SERCA pumps to resting oxygen consumption.
Data indicate that phospholamban (PLB) is not involved in heat generation and that sarcolipin (SLN) alone is responsible for muscle thermogenesis.
During mouse muscle development SLN is highly expressed in embryonic muscle and plays role in regulation of sarcoplasmic reticulum Ca(2+) stores during muscle differentiation
data collectively suggest that SLN is an important mediator of muscle thermogenesis and whole-body energy metabolism
ablation of SLN results in increased SERCA activity and sarcoplasmic reticulum Ca(2+) load, which, in turn, could cause abnormal intracellular Ca(2+) handling and atrial remodeling.
These results show that sarcolepin (SLN) regulates Ca(2+)-ATPase activity, the functional significance of SLN is graded to the SLN expression level, and SLN inhibitory effects on SERCA function are relieved in response to repeated contractions.
Dynamic regulation of the SERCA pump by phospholamban and/or sarcolipin maintains cardiac contractility in normal conditions and during pathophysiological states.
sarcolipin is likely to be an atrial chamber-specific regulator of Ca2+ cycling in heart
SLN overexpression inhibits SERCA2a through stabilization of SERCA2a-phospholamban interaction in the absence of PLN.
retention of sarcolipin in the endoplasmic reticulum is mediated through its association with other components through the C-terminal RSYQY sequence
Structure-Function Relationship of the SERCA Pump and Its Regulation by Phospholamban and Sarcolipin.
Self-assembling study of sarcolipin and its mutants in multiple molecular dynamic simulations has been reported.
These results suggest that sAnk1 interacts with SLN both directly and in complex with SERCA1 and reduces SLN's inhibitory effect on SERCA1 activity.
analysis of transmembrane dynamics of the Thr-5 phosphorylated sarcolipin pentameric channel
Phospholamban and sarcolipin are membrane proteins that differentially regulate SERCA function. (Review)
Molecular dynamics simulations help to clarify and to understand better the SLN pentamer channel that had a hydrophobic gate and could switch Na(+) and Cl(-) ion permeability by hydrated and vacuum states.
Although SLN and PLB binding to SERCA have different functional outcomes on the coupling efficiency of SERCA, both proteins decrease the apparent Ca(2+) affinity of the pump, suggesting that SLN and PLB inhibit SERCA by using a similar mechanism.
The C-terminal tail of SLN is a distinct, essential domain in the regulation of SERCA.
The selective downregulation of SLN and enhanced sarcoplasmic reticulum Ca(2+) uptake in human AF suggest that SLN downregulation could play an important role in abnormal intracellular Ca(2+) cycling in atrial pathology.
sarcolipin binds to phospholamban and inhibits polymerization
role in regulating sarco(endo)plasmic reticulum Ca2+-ATPase by binding to transmembrane helices alone or in association with phospholamban
Gene expression of SLN was studied in children with congenital heart defects.
Cell functions regulated by protein-protein interactions of the SERCA1a-sarcolipin complex is accomplished via s-palmitoylation and s-oleoylation of sarcolipin.
The expression of SLN and PLB mRNA and protein relative to SERCA1 or SERCA2 was assessed in ventricle, atrium, and skeltal msucle of mouse, rat, rabbit and pig.
Sarcoplasmic reticulum Ca(2+)-ATPases are transmembrane proteins that catalyze the ATP-dependent transport of Ca(2+) from the cytosol into the lumen of the sarcoplasmic reticulum in muscle cells. This gene encodes a small proteolipid that regulates several sarcoplasmic reticulum Ca(2+)-ATPases. The transmembrane protein interacts with Ca(2+)-ATPases and reduces the accumulation of Ca(2+) in the sarcoplasmic reticulum without affecting the rate of ATP hydrolysis.