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
We have identified a new human cDNA (y+L amino acid transporter-1 (y+LAT-1)) that induces system y+L transport activity with 4F2hc (the surface antigen 4F2 heavy chain) in oocytes. Human y+LAT-1 is a new member of a family of polytopic transmembrane proteins that are homologous to the yeast high aff...
| Autores: | , , , , , , , |
|---|---|
| Tipo de recurso: | artículo |
| Estado: | Versión publicada |
| Fecha de publicación: | 1998 |
| País: | España |
| Institución: | Universidad de Barcelona |
| Repositorio: | Dipòsit Digital de la UB |
| OAI Identifier: | oai:diposit.ub.edu:2445/176951 |
| Acceso en línea: | https://hdl.handle.net/2445/176951 |
| Access Level: | acceso abierto |
| Palabra clave: | Aminoàcids Metabolisme Errors congènits del metabolisme Genètica Antígens Proteïnes portadores Lisina Orina Amino acids Metabolism Inborn errors of metabolism Genetics Antigens Carrier proteins Lysine Urine |
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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 intoleranceTorrents Arenales, DavidEstévez Povedano, RaúlPineda Riu, MartaFernández, EsperanzaLloberas Cavero, JorgeShi, Yun-BoZorzano Olarte, AntonioPalacín Prieto, ManuelAminoàcidsMetabolismeErrors congènits del metabolismeGenèticaAntígensProteïnes portadoresLisinaOrinaAmino acidsMetabolismInborn errors of metabolismGeneticsAntigensCarrier proteinsLysineUrineWe have identified a new human cDNA (y+L amino acid transporter-1 (y+LAT-1)) that induces system y+L transport activity with 4F2hc (the surface antigen 4F2 heavy chain) in oocytes. Human y+LAT-1 is a new member of a family of polytopic transmembrane proteins that are homologous to the yeast high affinity methionine permease MUP1. Other members of this family, the Xenopus laevis IU12 and the human KIAA0245 cDNAs, also co-express amino acid transport activity with 4F2hc in oocytes, with characteristics that are compatible with those of systems L and y+L, respectively. y+LAT-1 protein forms a approximately 135-kDa, disulfide bond-dependent heterodimer with 4F2hc in oocytes, which upon reduction results in two protein bands of approximately 85 kDa (i.e. 4F2hc) and approximately 40 kDa (y+LAT-1). Mutation of the human 4F2hc residue cysteine 109 (Cys-109) to serine abolishes the formation of this heterodimer and drastically reduces the co-expressed transport activity. These data suggest that y+LAT-1 and other members of this family are different 4F2 light chain subunits, which associated with 4F2hc, constitute different amino acid transporters. Human y+LAT-1 mRNA is expressed in kidney >> peripheral blood leukocytes >> lung > placenta = spleen > small intestine. The human y+LAT-1 gene localizes at chromosome 14q11.2 (17cR approximately 374 kb from D14S1350), within the lysinuric protein intolerance (LPI) locus (Lauteala, T., Sistonen, P. , Savontaus, M. L., Mykkanen, J., Simell, J., Lukkarinen, M., Simmell, O., and Aula, P. (1997) Am. J. Hum. Genet. 60, 1479-1486). LPI is an inherited autosomal disease characterized by a defective dibasic amino acid transport in kidney, intestine, and other tissues. The pattern of expression of human y+LAT-1, its co-expressed transport activity with 4F2hc, and its chromosomal location within the LPI locus, suggest y+LAT-1 as a candidate gene for LPI.American Society for Biochemistry and Molecular Biology1998info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionapplication/pdfhttps://hdl.handle.net/2445/176951Articles publicats en revistes (Ciències Fisiològiques)reponame:Dipòsit Digital de la UBinstname:Universidad de BarcelonaInglésReproducció del document publicat a: https://doi.org/10.1074/jbc.273.49.32437Journal of Biological Chemistry, 1998, vol. 273, num. 49, p. 32437-32445https://doi.org/10.1074/jbc.273.49.32437(c) American Society for Biochemistry and Molecular Biology, 1998info:eu-repo/semantics/openAccessoai:diposit.ub.edu:2445/1769512026-05-27T06:46:51Z |
| dc.title.none.fl_str_mv |
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 |
| title |
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 |
| spellingShingle |
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 Torrents Arenales, David Aminoàcids Metabolisme Errors congènits del metabolisme Genètica Antígens Proteïnes portadores Lisina Orina Amino acids Metabolism Inborn errors of metabolism Genetics Antigens Carrier proteins Lysine Urine |
| title_short |
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 |
| title_full |
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 |
| title_fullStr |
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 |
| title_full_unstemmed |
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 |
| title_sort |
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 |
| dc.creator.none.fl_str_mv |
Torrents Arenales, David Estévez Povedano, Raúl Pineda Riu, Marta Fernández, Esperanza Lloberas Cavero, Jorge Shi, Yun-Bo Zorzano Olarte, Antonio Palacín Prieto, Manuel |
| author |
Torrents Arenales, David |
| author_facet |
Torrents Arenales, David Estévez Povedano, Raúl Pineda Riu, Marta Fernández, Esperanza Lloberas Cavero, Jorge Shi, Yun-Bo Zorzano Olarte, Antonio Palacín Prieto, Manuel |
| author_role |
author |
| author2 |
Estévez Povedano, Raúl Pineda Riu, Marta Fernández, Esperanza Lloberas Cavero, Jorge Shi, Yun-Bo Zorzano Olarte, Antonio Palacín Prieto, Manuel |
| author2_role |
author author author author author author author |
| dc.subject.none.fl_str_mv |
Aminoàcids Metabolisme Errors congènits del metabolisme Genètica Antígens Proteïnes portadores Lisina Orina Amino acids Metabolism Inborn errors of metabolism Genetics Antigens Carrier proteins Lysine Urine |
| topic |
Aminoàcids Metabolisme Errors congènits del metabolisme Genètica Antígens Proteïnes portadores Lisina Orina Amino acids Metabolism Inborn errors of metabolism Genetics Antigens Carrier proteins Lysine Urine |
| description |
We have identified a new human cDNA (y+L amino acid transporter-1 (y+LAT-1)) that induces system y+L transport activity with 4F2hc (the surface antigen 4F2 heavy chain) in oocytes. Human y+LAT-1 is a new member of a family of polytopic transmembrane proteins that are homologous to the yeast high affinity methionine permease MUP1. Other members of this family, the Xenopus laevis IU12 and the human KIAA0245 cDNAs, also co-express amino acid transport activity with 4F2hc in oocytes, with characteristics that are compatible with those of systems L and y+L, respectively. y+LAT-1 protein forms a approximately 135-kDa, disulfide bond-dependent heterodimer with 4F2hc in oocytes, which upon reduction results in two protein bands of approximately 85 kDa (i.e. 4F2hc) and approximately 40 kDa (y+LAT-1). Mutation of the human 4F2hc residue cysteine 109 (Cys-109) to serine abolishes the formation of this heterodimer and drastically reduces the co-expressed transport activity. These data suggest that y+LAT-1 and other members of this family are different 4F2 light chain subunits, which associated with 4F2hc, constitute different amino acid transporters. Human y+LAT-1 mRNA is expressed in kidney >> peripheral blood leukocytes >> lung > placenta = spleen > small intestine. The human y+LAT-1 gene localizes at chromosome 14q11.2 (17cR approximately 374 kb from D14S1350), within the lysinuric protein intolerance (LPI) locus (Lauteala, T., Sistonen, P. , Savontaus, M. L., Mykkanen, J., Simell, J., Lukkarinen, M., Simmell, O., and Aula, P. (1997) Am. J. Hum. Genet. 60, 1479-1486). LPI is an inherited autosomal disease characterized by a defective dibasic amino acid transport in kidney, intestine, and other tissues. The pattern of expression of human y+LAT-1, its co-expressed transport activity with 4F2hc, and its chromosomal location within the LPI locus, suggest y+LAT-1 as a candidate gene for LPI. |
| publishDate |
1998 |
| dc.date.none.fl_str_mv |
1998 |
| dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion |
| format |
article |
| status_str |
publishedVersion |
| dc.identifier.none.fl_str_mv |
https://hdl.handle.net/2445/176951 |
| url |
https://hdl.handle.net/2445/176951 |
| dc.language.none.fl_str_mv |
Inglés |
| language_invalid_str_mv |
Inglés |
| dc.relation.none.fl_str_mv |
Reproducció del document publicat a: https://doi.org/10.1074/jbc.273.49.32437 Journal of Biological Chemistry, 1998, vol. 273, num. 49, p. 32437-32445 https://doi.org/10.1074/jbc.273.49.32437 |
| dc.rights.none.fl_str_mv |
(c) American Society for Biochemistry and Molecular Biology, 1998 info:eu-repo/semantics/openAccess |
| rights_invalid_str_mv |
(c) American Society for Biochemistry and Molecular Biology, 1998 |
| eu_rights_str_mv |
openAccess |
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application/pdf |
| dc.publisher.none.fl_str_mv |
American Society for Biochemistry and Molecular Biology |
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American Society for Biochemistry and Molecular Biology |
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Articles publicats en revistes (Ciències Fisiològiques) reponame:Dipòsit Digital de la UB instname:Universidad de Barcelona |
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Universidad de Barcelona |
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Dipòsit Digital de la UB |
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Dipòsit Digital de la UB |
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15.300719 |