| Structural highlights
Disease
YLAT1_HUMAN Lysinuric protein intolerance. The disease is caused by variants affecting the gene represented in this entry.
Function
YLAT1_HUMAN Heterodimer with SLC3A2, that functions as an antiporter which operates as an efflux route by exporting cationic amino acids from inside the cells in exchange with neutral amino acids plus sodium ions and may participate in nitric oxide synthesis via the transport of L-arginine (PubMed:10080182, PubMed:10655553, PubMed:14603368, PubMed:15756301, PubMed:15776427, PubMed:17329401, PubMed:9829974, PubMed:9878049). Also mediates arginine transport in non-polarized cells, such as monocytes, and is essential for the correct function of these cells (PubMed:15280038, PubMed:31705628). The transport mechanism is electroneutral and operates with a stoichiometry of 1:1 (By similarity). In vitro, Na(+) and Li(+), but also H(+), are cotransported with the neutral amino acids (By similarity).[UniProtKB:Q9R0S5][1] [2] [3] [4] [5] [6] [7] [8] [9] [10]
References
- ↑ Torrents D, Mykkänen J, Pineda M, Feliubadaló L, Estévez R, de Cid R, Sanjurjo P, Zorzano A, Nunes V, Huoponen K, Reinikainen A, Simell O, Savontaus ML, Aula P, Palacín M. Identification of SLC7A7, encoding y+LAT-1, as the lysinuric protein intolerance gene. Nat Genet. 1999 Mar;21(3):293-6. PMID:10080182 doi:10.1038/6809
- ↑ Mykkänen J, Torrents D, Pineda M, Camps M, Yoldi ME, Horelli-Kuitunen N, Huoponen K, Heinonen M, Oksanen J, Simell O, Savontaus ML, Zorzano A, Palacín M, Aula P. Functional analysis of novel mutations in y(+)LAT-1 amino acid transporter gene causing lysinuric protein intolerance (LPI). Hum Mol Genet. 2000 Feb 12;9(3):431-8. PMID:10655553 doi:10.1093/hmg/9.3.431
- ↑ Arancibia-Garavilla Y, Toledo F, Casanello P, Sobrevia L. Nitric oxide synthesis requires activity of the cationic and neutral amino acid transport system y+L in human umbilical vein endothelium. Exp Physiol. 2003 Nov;88(6):699-710. PMID:14603368
- ↑ Rotoli BM, Bussolati O, Sala R, Barilli A, Talarico E, Gazzola GC, Dall'Asta V. INFgamma stimulates arginine transport through system y+L in human monocytes. FEBS Lett. 2004 Jul 30;571(1-3):177-81. PMID:15280038 doi:10.1016/j.febslet.2004.06.086
- ↑ Sperandeo MP, Paladino S, Maiuri L, Maroupulos GD, Zurzolo C, Taglialatela M, Andria G, Sebastio G. A y(+)LAT-1 mutant protein interferes with y(+)LAT-2 activity: implications for the molecular pathogenesis of lysinuric protein intolerance. Eur J Hum Genet. 2005 May;13(5):628-34. PMID:15756301 doi:10.1038/sj.ejhg.5201376
- ↑ Sperandeo MP, Annunziata P, Ammendola V, Fiorito V, Pepe A, Soldovieri MV, Taglialatela M, Andria G, Sebastio G. Lysinuric protein intolerance: identification and functional analysis of mutations of the SLC7A7 gene. Hum Mutat. 2005 Apr;25(4):410. PMID:15776427 doi:10.1002/humu.9323
- ↑ Rotmann A, Simon A, Martiné U, Habermeier A, Closs EI. Activation of classical protein kinase C decreases transport via systems y+ and y+L. Am J Physiol Cell Physiol. 2007 Jun;292(6):C2259-68. PMID:17329401 doi:10.1152/ajpcell.00323.2006
- ↑ Rotoli BM, Barilli A, Visigalli R, Ferrari F, Dall'Asta V. y+LAT1 and y+LAT2 contribution to arginine uptake in different human cell models: Implications in the pathophysiology of Lysinuric Protein Intolerance. J Cell Mol Med. 2020 Jan;24(1):921-929. PMID:31705628 doi:10.1111/jcmm.14801
- ↑ Torrents D, Estevez R, Pineda M, Fernandez E, Lloberas J, Shi YB, Zorzano A, Palacin M. Identification and characterization of a membrane protein (y+L amino acid transporter-1) that associates with 4F2hc to encode the amino acid transport activity y+L. A candidate gene for lysinuric protein intolerance. J Biol Chem. 1998 Dec 4;273(49):32437-45. PMID:9829974
- ↑ Pfeiffer R, Rossier G, Spindler B, Meier C, Kuhn L, Verrey F. Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family. EMBO J. 1999 Jan 4;18(1):49-57. PMID:9878049 doi:https://dx.doi.org/10.1093/emboj/18.1.49
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