Mutation of the 4F2 heavy-chain carboxy terminus causes y⁺LAT2 light-chain dysfunction

References

• 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; 355: 725–731
   PubMed Web of Science ®Google Scholar
• Broer A, Hamprecht B, Broer S. Discrimination of two amino acid transport activities in 4F2 heavy chain-expressing Xenopus laevis oocytes. Biochem J 1998a; 333: 549–554
   PubMed Web of Science ®Google Scholar
• 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; 349: 787–795
   PubMed Web of Science ®Google Scholar
• Broer S. Xenopus laevis oocytes. Methods Mol Biol 2003; 227: 245–258
   PubMedGoogle Scholar
• Broer S, Broer A, Hamprecht B. The 4F2hc surface antigen is necessary for expression of system L-like neutral amino acid-transport activity in C6-BU-1 rat glioma cells: evidence from expression studies in Xenopus laevis oocytes. Biochem J 1995; 312: 863–870
   PubMed Web of Science ®Google Scholar
• Broer S, Schneider HP, Broer A, Rahman B, Hamprecht B, Deitmer JW. Characterization of the monocarboxylate transporter 1 expressed in Xenopus laevis oocytes by changes in cytosolic pH. Biochem J 1998b; 333: 167–174
   PubMed Web of Science ®Google Scholar
• Broer S, Wagner CA. Structure-function relationships of heterodimeric amino acid transporters. Cell Biochem Biophys 2002; 36: 155–168
   PubMed Web of Science ®Google Scholar
• Busch AE, Herzer T, Waldegger S, Schmidt F, Palacin M, Biber J, Markovich D, Murer H, Lang F. Opposite directed currents induced by the transport of dibasic and neutral amino acids in Xenopus oocytes expressing the protein rBAT. J Biol Chem 1994; 269: 25581–25586
   PubMed Web of Science ®Google Scholar
• Chillaron J, Bertran J, Palacin M. Heteromeric amino acid transporters:cystinuria and lysinuric protein intolerance. Membrane Transporter Diseases, S Broer, CA Wagner. Kluwer Academic/Plenum Publishers, New York 2004; 207–231
   Google Scholar
• Chillaron J, Estevez R, Samarzija I, Waldegger S, Testar X, Lang F, Zorzano A, Busch A, Palacin M. An intracellular trafficking defect in type I cystinuria rBAT mutants M467T and M467K. J Biol Chem 1997; 272: 9543–9549
   PubMed Web of Science ®Google Scholar
• Chillaron J, Roca R, Valencia A, Zorzano A, Palacin M. Heteromeric amino acid transporters: biochemistry, genetics, and physiology. Am J Physiol Renal Physiol 2001; 281: F995–F1018
   Web of Science ®Google Scholar
• Coady MJ, Chen XZ, Lapointe JY. rBAT is an amino acid exchanger with variable stoichiometry. J Membr Biol 1996; 149: 1–8
   PubMed Web of Science ®Google Scholar
• Fenczik CA, Sethi T, Ramos JW, Hughes PE, Ginsberg MH. Complementation of dominant suppression implicates CD98 in integrin activation [see comments]. Nature 1997; 390: 81–85
   PubMed Web of Science ®Google Scholar
• Fenczik CA, Zent R, Dellos M, Calderwood DA, Satriano J, Kelly C, Ginsberg MH. Distinct domains of CD98hc regulate integrins and amino acid transport. J Biol Chem 2001; 276: 8746–8752
   PubMed Web of Science ®Google Scholar
• Franca R, Veljkovic E, Walter S, Wagner CA, Verrey F. Heterodimeric amino acid transporter glycoprotein domains determining functional subunit association. Biochem J 2005; 388: 435–443
   PubMed Web of Science ®Google Scholar
• Gasol E, Jimenez-Vidal M, Chillaron J, Zorzano A, Palacin M. Membrane topology of system xc-light subunit reveals a re-entrant loop with substrate-restricted accessibility. J Biol Chem 2004; 279: 31228–31236
   PubMed Web of Science ®Google Scholar
• Henderson NC, Collis EA, Mackinnon AC, Simpson KJ, Haslett C, Zent R, Ginsberg M, Sethi T. CD98hc (SLC3A2) interaction with beta 1 integrins is required for transformation. J Biol Chem 2004; 279: 54731–54741
   PubMed Web of Science ®Google Scholar
• Horton RM, Hunt HD, Ho SN, Pullen JK, Pease LR. Engineering hybrid genes without the use of restriction enzymes: gene splicing by overlap extension. Gene 1989; 77: 61–68
   PubMed Web of Science ®Google Scholar
• Mastroberardino L, Spindler B, Pfeiffer R, Skelly PJ, Loffing J, Shoemaker CB, Verrey F. Amino-acid transport by heterodimers of 4F2hc/CD98 and members of a permease family. Nature 1998; 395: 288–291
   PubMed Web of Science ®Google Scholar
• Mora C, Chillaron J, Calonge MJ, Forgo J, Testar X, Nunes V, Murer H, Zorzano A, Palacin M. The rBAT gene is responsible for L-cystine uptake via the b0,(+)-like amino acid transport system in a “renal proximal tubular” cell line (OK cells). J Biol Chem 1996; 271: 10569–10576
   PubMed Web of Science ®Google Scholar
• Palacin M, Bertran J, Chillaron J, Estevez R, Zorzano A. Lysinuric protein intolerance: mechanisms of pathophysiology. Mol Genet Metab 2004; 81 (Suppl.): 27–37
   Web of Science ®Google Scholar
• Palacin M, Kanai Y. The ancillary proteins of HATs: SLC3 family of amino acid transporters. Pflugers Arch 2004; 447: 490–494
   PubMed Web of Science ®Google Scholar
• Palmieri F, Indiveri C, Bisaccia F, Kramer R. Functional properties of purified and reconstituted mitochondrial metabolite carriers. J Bioenerg Biomembr 1993; 25: 525–535
   PubMed Web of Science ®Google Scholar
• Peter GJ, Panova TB, Christie GR, Taylor PM. Cysteine residues in the C-terminus of the neutral- and basic-amino-acid transporter heavy-chain subunit contribute to functional properties of the system b0,+-type amino acid transporter. Biochem J 2000; 351: 677–682
   PubMed Web of Science ®Google Scholar
• 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; 18: 49–57
   PubMed Web of Science ®Google Scholar
• Pineda M, Wagner CA, Broer A, Stehberger PA, Kaltenbach S, Gelpi JL, Martin Del Rio R, Zorzano A, Palacin M, Lang F, et al. Cystinuria-specific rBAT(R365W) mutation reveals two translocation pathways in the amino acid transporter rBAT-b0,+AT. Biochem J 2004; 377: 665–674
   PubMed Web of Science ®Google Scholar
• Reig N, Chillaron J, Bartoccioni P, Fernandez E, Bendahan A, Zorzano A, Kanner B, Palacin M, Bertran J. The light subunit of system b(o,+) is fully functional in the absence of the heavy subunit. Embo J 2002; 21: 4906–4914
   PubMed Web of Science ®Google Scholar
• Rintoul RC, Buttery RC, Mackinnon AC, Wong WS, Mosher D, Haslett C, Sethi T. Cross-linking CD98 promotes integrin-like signaling and anchorage-independent growth. Mol Biol Cell 2002; 13: 2841–2852
   PubMed Web of Science ®Google Scholar
• Torras-Llort M, Torrents D, Soriano-Garcia JF, Gelpi JL, Estevez R, Ferrer R, Palacin M, Moreto M. Sequential amino acid exchange across b(0,+)-like system in chicken brush border jejunum. J Membr Biol 2001; 180: 213–220
   PubMed Web of Science ®Google Scholar
• 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; 273: 32437–32445
   PubMed Web of Science ®Google Scholar
• Verrey F, Closs EI, Wagner CA, Palacin M, Endou H, Kanai Y. CATs and HATs: the SLC7 family of amino acid transporters. Pflugers Arch 2004; 447: 532–542
   PubMed Web of Science ®Google Scholar
• Wagner CA, Lang F, Broer S. Function and structure of heterodimeric amino acid transporters. Am J Physiol Cell Physiol 2001; 281: C1077–1093
   PubMed Web of Science ®Google Scholar
• Watanabe K, Hata Y, Kizaki H, Katsube Y, Suzuki Y. The refined crystal structure of Bacillus cereus oligo-1,6-glucosidase at 2.0 A resolution: structural characterization of proline-substitution sites for protein thermostabilization. J Mol Biol 1997; 269: 142–153
   PubMed Web of Science ®Google Scholar