Protein-coding gene in the species Homo sapiens
Sarcolipin is amicropeptide protein that in humans is encoded by theSLN gene .[ 3] [ 4]
Sarcoplasmic reticulum Ca2+ -ATPases are transmembrane proteins that catalyze theATP -dependent transport ofCa2+ from the cytosol into the lumen of thesarcoplasmic reticulum in muscle cells. The SLN gene encodes a small transmembrane proteolipid that regulates several sarcoplasmic reticulum Ca2+ -ATPases by reducing the accumulation of Ca2+ in the sarcoplasmic reticulum without affecting the rate of ATP hydrolysis.[ 4]
Ablation of sarcolipin increases atrial Ca2+ transient amplitudes and enhancedatrial contractility . Furthermore, atria from sarcolipin-null mice have blunted response toisoproterenol stimulation, implicating sarcolipin as a mediator ofbeta-adrenergic responses in atria.[ 5]
Sarcolipin is an important mediator of muscle based non shivering thermogenesis (NST). It causes thesarcoplasmic reticulum Ca2+ -ATPases to stop pumping Ca2+ ions but continue futilely hydrolysing ATP, thus releasing the energy as heat.[ 6] [ 7] Sarcolipin mediated heat production is very important for many organisms to maintain a warm body. In mammals thermogenesis by skeletal muscles is complemented by thermogenesis in thebrown adipose tissue and beige adipose tissue.[ 8] Sarcolipin mediated heat production in contractile muscles helps endothermic fish like theopah heat its body. Some fishes like thebillfishes have a specialised brain heater tissue that is derived from muscles that cannot contract but specialise in producing heat using sarcolipin.
SLN (gene) has been shown tointeract withPLN [ 9] [ 10] andATP2A1 .[ 9] [ 10]
^a b c GRCh38: Ensembl release 89: ENSG00000170290 –Ensembl , May 2017^ "Human PubMed Reference:" .National Center for Biotechnology Information, U.S. National Library of Medicine .^ Odermatt A, Taschner PE, Scherer SW, Beatty B, Khanna VK, Cornblath DR, et al. (November 1997)."Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease" .Genomics .45 (3):541– 53.doi :10.1006/geno.1997.4967 .hdl :2066/25426 .PMID 9367679 .S2CID 41989102 . ^a b "Entrez Gene: SLN sarcolipin" .^ Babu GJ, Bhupathy P, Timofeyev V, Petrashevskaya NN, Reiser PJ, Chiamvimonvat N, Periasamy M (November 2007)."Ablation of sarcolipin enhances sarcoplasmic reticulum calcium transport and atrial contractility" .Proceedings of the National Academy of Sciences of the United States of America .104 (45):17867– 72.Bibcode :2007PNAS..10417867B .doi :10.1073/pnas.0707722104 .PMC 2077025 .PMID 17971438 . ^ Bal NC, Periasamy M (March 2020)."Uncoupling of sarcoendoplasmic reticulum calcium ATPase pump activity by sarcolipin as the basis for muscle non-shivering thermogenesis" .Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences .375 (1793): 20190135.doi :10.1098/rstb.2019.0135 .PMC 7017432 .PMID 31928193 . ^ Legendre LJ, Davesne D (March 2020)."The evolution of mechanisms involved in vertebrate endothermy" .Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences .375 (1793): 20190136.doi :10.1098/rstb.2019.0136 .PMC 7017440 .PMID 31928191 . ^ Reilly SM, Saltiel RA (22 October 2015)."A Futile Approach to Fighting Obesity?" .Cell .163 (3):539– 540.doi :10.1016/j.cell.2015.10.006 .PMID 26496598 .S2CID 10336243 . ^a b Asahi M, Sugita Y, Kurzydlowski K, De Leon S, Tada M, Toyoshima C, MacLennan DH (April 2003)."Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban" .Proceedings of the National Academy of Sciences of the United States of America .100 (9):5040– 5.Bibcode :2003PNAS..100.5040A .doi :10.1073/pnas.0330962100 .PMC 154294 .PMID 12692302 . ^a b Asahi M, Kurzydlowski K, Tada M, MacLennan DH (July 2002)."Sarcolipin inhibits polymerization of phospholamban to induce superinhibition of sarco(endo)plasmic reticulum Ca2+-ATPases (SERCAs)" .The Journal of Biological Chemistry .277 (30):26725– 8.doi :10.1074/jbc.C200269200 .PMID 12032137 .
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