| Structural highlights
Function
YLAT2_HUMAN Heterodimer with SLC3A2, that functions as an antiporter which operates as an efflux route by exporting cationic amino acids such as L-arginine from inside the cells in exchange with neutral amino acids like L-leucine, L-glutamine and isoleucine, plus sodium ions and may participate in nitric oxide synthesis (PubMed:10903140, PubMed:11311135, PubMed:14603368, PubMed:15756301, PubMed:16785209, PubMed:17329401, PubMed:19562367, PubMed:31705628, PubMed:9829974). Also exchanges L-arginine with L-lysine in a sodium-independent manner (PubMed:10903140). The transport mechanism is electroneutral and operates with a stoichiometry of 1:1 (PubMed:10903140). Contributes to ammonia-induced increase of L-arginine uptake in cerebral cortical astrocytes leading to ammonia-dependent increase of nitric oxide (NO) production via inducible nitric oxide synthase (iNOS) induction, and protein nitration (By similarity). May mediate transport of ornithine in retinal pigment epithelial (RPE) cells (PubMed:17197568). May also transport glycine betaine in a sodium dependent manner from the cumulus granulosa into the enclosed oocyte (By similarity).[UniProtKB:D3ZMM8][UniProtKB:Q8BGK6][1] [2] [3] [4] [5] [6] [7] [8] [9] [10]
References
- ↑ Broer A, Wagner CA, Lang F, Broer S. The heterodimeric amino acid transporter 4F2hc/y+LAT2 mediates arginine efflux in exchange with glutamine. Biochem J. 2000 Aug 1;349 Pt 3:787-95. PMID:10903140
- ↑ Broer A, Friedrich B, Wagner CA, Fillon S, Ganapathy V, Lang F, Broer S. Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires different domains. Biochem J. 2001 May 1;355(Pt 3):725-31. PMID:11311135
- ↑ 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
- ↑ 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
- ↑ Chubb S, Kingsland AL, Bröer A, Bröer S. Mutation of the 4F2 heavy-chain carboxy terminus causes y+ LAT2 light-chain dysfunction. Mol Membr Biol. 2006 May-Jun;23(3):255-67. PMID:16785209 doi:10.1080/09687860600652968
- ↑ Kaneko S, Ando A, Okuda-Ashitaka E, Maeda M, Furuta K, Suzuki M, Matsumura M, Ito S. Ornithine transport via cationic amino acid transporter-1 is involved in ornithine cytotoxicity in retinal pigment epithelial cells. Invest Ophthalmol Vis Sci. 2007 Jan;48(1):464-71. PMID:17197568 doi:10.1167/iovs.06-0398
- ↑ 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, Closs EI, Barilli A, Visigalli R, Simon A, Habermeier A, Bianchi N, Gambari R, Gazzola GC, Bussolati O, Dall'Asta V. Arginine transport in human erythroid cells: discrimination of CAT1 and 4F2hc/y+LAT2 roles. Pflugers Arch. 2009 Oct;458(6):1163-73. PMID:19562367 doi:10.1007/s00424-009-0692-9
- ↑ 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
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