sarcolipin

{{Short description|Protein-coding gene in the species Homo sapiens}}

{{Infobox_gene}}

Sarcolipin is a micropeptide protein that in humans is encoded by the SLN gene.{{cite journal | vauthors = Odermatt A, Taschner PE, Scherer SW, Beatty B, Khanna VK, Cornblath DR, Chaudhry V, Yee WC, Schrank B, Karpati G, Breuning MH, Knoers N, MacLennan DH | display-authors = 6 | title = Characterization of the gene encoding human sarcolipin (SLN), a proteolipid associated with SERCA1: absence of structural mutations in five patients with Brody disease | journal = Genomics | volume = 45 | issue = 3 | pages = 541–53 | date = November 1997 | pmid = 9367679 | doi = 10.1006/geno.1997.4967 | url = http://repub.eur.nl/pub/59319 | hdl = 2066/25426 | s2cid = 41989102 | hdl-access = free }}{{cite web | title = Entrez Gene: SLN sarcolipin| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=6588}}

Function

Sarcoplasmic reticulum Ca2+-ATPases are transmembrane proteins that catalyze the ATP-dependent transport of Ca2+ from the cytosol into the lumen of the sarcoplasmic 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.

Ablation of sarcolipin increases atrial Ca2+ transient amplitudes and enhanced atrial contractility. Furthermore, atria from sarcolipin-null mice have blunted response to isoproterenol stimulation, implicating sarcolipin as a mediator of beta-adrenergic responses in atria.{{cite journal | vauthors = Babu GJ, Bhupathy P, Timofeyev V, Petrashevskaya NN, Reiser PJ, Chiamvimonvat N, Periasamy M | title = Ablation of sarcolipin enhances sarcoplasmic reticulum calcium transport and atrial contractility | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 104 | issue = 45 | pages = 17867–72 | date = November 2007 | pmid = 17971438 | pmc = 2077025 | doi = 10.1073/pnas.0707722104 | bibcode = 2007PNAS..10417867B | doi-access = free }}

Sarcolipin is an important mediator of muscle based non shivering thermogenesis (NST). It causes the sarcoplasmic reticulum Ca2+-ATPases to stop pumping Ca2+ ions but continue futilely hydrolysing ATP, thus releasing the energy as heat.{{cite journal | vauthors = Bal NC, Periasamy M | title = Uncoupling of sarcoendoplasmic reticulum calcium ATPase pump activity by sarcolipin as the basis for muscle non-shivering thermogenesis | journal = Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences | volume = 375 | issue = 1793 | pages = 20190135 | date = March 2020 | pmid = 31928193 | doi = 10.1098/rstb.2019.0135 | url= | pmc = 7017432 }}{{cite journal | vauthors = Legendre LJ, Davesne D | title = The evolution of mechanisms involved in vertebrate endothermy | journal = Philosophical Transactions of the Royal Society of London. Series B, Biological Sciences | volume = 375 | issue = 1793 | pages = 20190136 | date = March 2020 | pmid = 31928191 | doi = 10.1098/rstb.2019.0136 | pmc = 7017440 | doi-access = free }} 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 the brown adipose tissue and beige adipose tissue. {{cite journal | vauthors = Reilly SM, Saltiel RA | title = A Futile Approach to Fighting Obesity? | journal = Cell | volume = 163 | issue = 3 | pages = 539–540 | date = 22 October 2015 | doi = 10.1016/j.cell.2015.10.006 | pmid = 26496598 | s2cid = 10336243 | doi-access = free }} Sarcolipin mediated heat production in contractile muscles helps endothermic fish like the opah heat its body. Some fishes like the billfishes have a specialised brain heater tissue that is derived from muscles that cannot contract but specialise in producing heat using sarcolipin.

Interactions

SLN (gene) has been shown to interact with PLN{{cite journal | vauthors = Asahi M, Sugita Y, Kurzydlowski K, De Leon S, Tada M, Toyoshima C, MacLennan DH | title = Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 100 | issue = 9 | pages = 5040–5 | date = April 2003 | pmid = 12692302 | pmc = 154294 | doi = 10.1073/pnas.0330962100 | bibcode = 2003PNAS..100.5040A | doi-access = free }}{{cite journal | vauthors = Asahi M, Kurzydlowski K, Tada M, MacLennan DH | title = Sarcolipin inhibits polymerization of phospholamban to induce superinhibition of sarco(endo)plasmic reticulum Ca2+-ATPases (SERCAs) | journal = The Journal of Biological Chemistry | volume = 277 | issue = 30 | pages = 26725–8 | date = July 2002 | pmid = 12032137 | doi = 10.1074/jbc.C200269200 | doi-access = free }} and ATP2A1.

References

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Further reading

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  • {{cite journal | vauthors = Lanfranchi G, Muraro T, Caldara F, Pacchioni B, Pallavicini A, Pandolfo D, Toppo S, Trevisan S, Scarso S, Valle G | display-authors = 6 | title = Identification of 4370 expressed sequence tags from a 3'-end-specific cDNA library of human skeletal muscle by DNA sequencing and filter hybridization | journal = Genome Research | volume = 6 | issue = 1 | pages = 35–42 | date = January 1996 | pmid = 8681137 | doi = 10.1101/gr.6.1.35 | doi-access = free }}
  • {{cite journal | vauthors = Odermatt A, Becker S, Khanna VK, Kurzydlowski K, Leisner E, Pette D, MacLennan DH | title = Sarcolipin regulates the activity of SERCA1, the fast-twitch skeletal muscle sarcoplasmic reticulum Ca2+-ATPase | journal = The Journal of Biological Chemistry | volume = 273 | issue = 20 | pages = 12360–9 | date = May 1998 | pmid = 9575189 | doi = 10.1074/jbc.273.20.12360 | doi-access = free }}
  • {{cite journal | vauthors = Smith WS, Broadbridge R, East JM, Lee AG | title = Sarcolipin uncouples hydrolysis of ATP from accumulation of Ca2+ by the Ca2+-ATPase of skeletal-muscle sarcoplasmic reticulum | journal = The Biochemical Journal | volume = 361 | issue = Pt 2 | pages = 277–86 | date = January 2002 | pmid = 11772399 | pmc = 1222307 | doi = 10.1042/0264-6021:3610277 }}
  • {{cite journal | vauthors = Mascioni A, Karim C, Barany G, Thomas DD, Veglia G | title = Structure and orientation of sarcolipin in lipid environments | journal = Biochemistry | volume = 41 | issue = 2 | pages = 475–82 | date = January 2002 | pmid = 11781085 | doi = 10.1021/bi011243m }}
  • {{cite journal | vauthors = Asahi M, Kurzydlowski K, Tada M, MacLennan DH | title = Sarcolipin inhibits polymerization of phospholamban to induce superinhibition of sarco(endo)plasmic reticulum Ca2+-ATPases (SERCAs) | journal = The Journal of Biological Chemistry | volume = 277 | issue = 30 | pages = 26725–8 | date = July 2002 | pmid = 12032137 | doi = 10.1074/jbc.C200269200 | doi-access = free }}
  • {{cite journal | vauthors = Minamisawa S, Wang Y, Chen J, Ishikawa Y, Chien KR, Matsuoka R | title = Atrial chamber-specific expression of sarcolipin is regulated during development and hypertrophic remodeling | journal = The Journal of Biological Chemistry | volume = 278 | issue = 11 | pages = 9570–5 | date = March 2003 | pmid = 12645548 | doi = 10.1074/jbc.M213132200 | doi-access = free }}
  • {{cite journal | vauthors = Asahi M, Sugita Y, Kurzydlowski K, De Leon S, Tada M, Toyoshima C, MacLennan DH | title = Sarcolipin regulates sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) by binding to transmembrane helices alone or in association with phospholamban | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 100 | issue = 9 | pages = 5040–5 | date = April 2003 | pmid = 12692302 | pmc = 154294 | doi = 10.1073/pnas.0330962100 | bibcode = 2003PNAS..100.5040A | doi-access = free }}
  • {{cite journal | vauthors = Suzuki Y, Yamashita R, Shirota M, Sakakibara Y, Chiba J, Mizushima-Sugano J, Nakai K, Sugano S | display-authors = 6 | title = Sequence comparison of human and mouse genes reveals a homologous block structure in the promoter regions | journal = Genome Research | volume = 14 | issue = 9 | pages = 1711–8 | date = September 2004 | pmid = 15342556 | pmc = 515316 | doi = 10.1101/gr.2435604 }}
  • {{cite journal | vauthors = Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M | display-authors = 6 | title = Towards a proteome-scale map of the human protein-protein interaction network | journal = Nature | volume = 437 | issue = 7062 | pages = 1173–8 | date = October 2005 | pmid = 16189514 | doi = 10.1038/nature04209 | bibcode = 2005Natur.437.1173R | s2cid = 4427026 }}
  • {{cite journal | vauthors = Vittorini S, Storti S, Parri MS, Cerillo AG, Clerico A | title = SERCA2a, phospholamban, sarcolipin, and ryanodine receptors gene expression in children with congenital heart defects | journal = Molecular Medicine | volume = 13 | issue = 1–2 | pages = 105–11 | year = 2007 | pmid = 17515962 | pmc = 1869624 | doi = 10.2119/2006-00054.Vittorini }}

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