Editing Leucine (section)

===Pharmacodynamics===
Leucine is a [[dietary]] [[amino acid]] with the capacity to directly stimulate [[myofibrillar]] muscle [[protein biosynthesis|protein synthesis]].<ref>{{cite journal | vauthors = Etzel MR | title = Manufacture and use of dairy protein fractions | journal = The Journal of Nutrition | volume = 134 | issue = 4 | pages = 996S–1002S | date = April 2004 | pmid = 15051860 | doi = 10.1093/jn/134.4.996S | doi-access = free }}</ref> This effect of leucine results from its role as an activator of the [[mechanistic target of rapamycin]] (mTOR),<ref name="Pharmacology of HMB-FA in humans in vivo" /> a [[serine-threonine protein kinase]] that regulates [[protein biosynthesis]] and [[cell growth]].  The activation of mTOR by leucine is mediated through [[Rag GTPase]]s,<ref name="pmid28963468">{{cite journal | vauthors = Kim JH, Lee C, Lee M, Wang H, Kim K, Park SJ, Yoon I, Jang J, Zhao H, Kim HK, Kwon NH, Jeong SJ, Yoo HC, Kim JH, Yang JS, Lee MY, Lee CW, Yun J, Oh SJ, Kang JS, Martinis SA, Hwang KY, Guo M, Han G, Han JM, Kim S | display-authors = 6 | title = Control of leucine-dependent mTORC1 pathway through chemical intervention of leucyl-tRNA synthetase and RagD interaction | journal = Nature Communications | volume = 8 | issue = 1 | pages = 732 | date = September 2017 | pmid = 28963468 | pmc = 5622079 | doi = 10.1038/s41467-017-00785-0 | bibcode = 2017NatCo...8..732K }}</ref><ref name="pmid23361334">{{cite journal | vauthors = Jewell JL, Russell RC, Guan KL | title = Amino acid signalling upstream of mTOR | journal = Nature Reviews. Molecular Cell Biology | volume = 14 | issue = 3 | pages = 133–39 | date = March 2013 | pmid = 23361334 | pmc = 3988467 | doi = 10.1038/nrm3522 }}</ref><ref name="pmid18497260">{{cite journal | vauthors = Sancak Y, Peterson TR, Shaul YD, Lindquist RA, Thoreen CC, Bar-Peled L, Sabatini DM | title = The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1 | journal = Science | volume = 320 | issue = 5882 | pages = 1496–501 | date = June 2008 | pmid = 18497260 | pmc = 2475333 | doi = 10.1126/science.1157535 | bibcode = 2008Sci...320.1496S }}</ref> leucine [[ligand binding|binding]] to [[leucyl-tRNA synthetase]],<ref name="pmid28963468" /><ref name="pmid23361334" /> leucine binding to [[sestrin 2]],<ref>{{cite journal | vauthors = Wolfson RL, Chantranupong L, Saxton RA, Shen K, Scaria SM, Cantor JR, Sabatini DM | title = Sestrin2 is a leucine sensor for the mTORC1 pathway | journal = Science | volume = 351 | issue = 6268 | pages = 43–48 | date = January 2016 | pmid = 26449471 | pmc = 4698017 | doi = 10.1126/science.aab2674 | bibcode = 2016Sci...351...43W }}</ref><ref>{{cite journal | vauthors = Saxton RA, Knockenhauer KE, Wolfson RL, Chantranupong L, Pacold ME, Wang T, Schwartz TU, Sabatini DM | display-authors = 6 | title = Structural basis for leucine sensing by the Sestrin2-mTORC1 pathway | journal = Science | volume = 351 | issue = 6268 | pages = 53–58 | date = January 2016 | pmid = 26586190 | pmc = 4698039 | doi = 10.1126/science.aad2087 | bibcode = 2016Sci...351...53S }}</ref><ref>{{cite journal | vauthors = Chantranupong L, Wolfson RL, Orozco JM, Saxton RA, Scaria SM, Bar-Peled L, Spooner E, Isasa M, Gygi SP, Sabatini DM | display-authors = 6 | title = The Sestrins interact with GATOR2 to negatively regulate the amino-acid-sensing pathway upstream of mTORC1 | journal = Cell Reports | volume = 9 | issue = 1 | pages = 1–8 | date = October 2014 | pmid = 25263562 | pmc = 4223866 | doi = 10.1016/j.celrep.2014.09.014 }}</ref> and possibly other mechanisms.