Luminal heterodimeric amino acid transporter defective in cystinuria
Mutations of the glycoprotein rBAT cause cystinuria type I, an autosomal recessive failure of dibasic amino acid transport (b(0,+) type) across luminal membranes of intestine and kidney cells. Here we identify the permease-like protein b(0,+)AT as the catalytic subunit that associates by a disulfide...
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| Veröffentlicht in: | Molecular biology of the cell 1999-12, Vol.10 (12), p.4135-4147 |
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| creator | Pfeiffer, R Loffing, J Rossier, G Bauch, C Meier, C Eggermann, T Loffing-Cueni, D Kühn, L C Verrey, F |
| description | Mutations of the glycoprotein rBAT cause cystinuria type I, an autosomal recessive failure of dibasic amino acid transport (b(0,+) type) across luminal membranes of intestine and kidney cells. Here we identify the permease-like protein b(0,+)AT as the catalytic subunit that associates by a disulfide bond with rBAT to form a hetero-oligomeric b(0,+) amino acid transporter complex. We demonstrate its b(0,+)-type amino acid transport kinetics using a heterodimeric fusion construct and show its luminal brush border localization in kidney proximal tubule. These biochemical, transport, and localization characteristics as well as the chromosomal localization on 19q support the notion that the b(0,+)AT protein is the product of the gene defective in non-type I cystinuria. |
| doi_str_mv | 10.1091/mbc.10.12.4135 |
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Here we identify the permease-like protein b(0,+)AT as the catalytic subunit that associates by a disulfide bond with rBAT to form a hetero-oligomeric b(0,+) amino acid transporter complex. We demonstrate its b(0,+)-type amino acid transport kinetics using a heterodimeric fusion construct and show its luminal brush border localization in kidney proximal tubule. 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These biochemical, transport, and localization characteristics as well as the chromosomal localization on 19q support the notion that the b(0,+)AT protein is the product of the gene defective in non-type I cystinuria.</description><subject>Amino Acid Sequence</subject><subject>Amino Acid Transport Systems</subject><subject>Amino Acid Transport Systems, Basic</subject><subject>Amino Acids - metabolism</subject><subject>Animals</subject><subject>Biological Transport</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>Chromosomes, Human, Pair 19</subject><subject>Cloning, Molecular</subject><subject>Cystinuria - genetics</subject><subject>Cystinuria - metabolism</subject><subject>Fluorescent Antibody Technique</subject><subject>Humans</subject><subject>In Situ Hybridization</subject><subject>Kidney - metabolism</subject><subject>Kidney - ultrastructure</subject><subject>Male</subject><subject>Membrane Glycoproteins - genetics</subject><subject>Membrane Glycoproteins - metabolism</subject><subject>Mice</subject><subject>Microvilli - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Oocytes - metabolism</subject><subject>Organ Specificity</subject><subject>Sequence Alignment</subject><subject>Xenopus laevis</subject><issn>1059-1524</issn><issn>1939-4586</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUE1LAzEUDKLYWr16lD1525rvTcCL-A0FL3oO2SRrI7ubmuwW-u9NbZF6esObmfeGAeASwTmCEt10tZlvMZ5TRNgRmCJJZEmZ4McZQyZLxDCdgLOUviBElPLqFEwyIQSnYgoeFmPne90WSze4GKzvXPSm0HkZCm28LYao-7QKMdOFdY0zg1-7wveF2aTB92P0-hycNLpN7mI_Z-Dj6fH9_qVcvD2_3t8tSkMFHkoiGdXEGi6xZrXUlaVa5Hi84kbmaIJzgVHVcFtzjrTFosENNxTiilpHHJmB293d1Vh3zhrX53CtWkXf6bhRQXv1n-n9Un2GtcKsoiLbr_f2GL5HlwbV-WRc2-rehTEpLgnFELEsnO-EJoaUomv-XiCotrWrXPsvxmpbezZcHQY7kO96Jj-GW3_P</recordid><startdate>19991201</startdate><enddate>19991201</enddate><creator>Pfeiffer, R</creator><creator>Loffing, J</creator><creator>Rossier, G</creator><creator>Bauch, C</creator><creator>Meier, C</creator><creator>Eggermann, T</creator><creator>Loffing-Cueni, D</creator><creator>Kühn, L C</creator><creator>Verrey, F</creator><general>The American Society for Cell Biology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19991201</creationdate><title>Luminal heterodimeric amino acid transporter defective in cystinuria</title><author>Pfeiffer, R ; Loffing, J ; Rossier, G ; Bauch, C ; Meier, C ; Eggermann, T ; Loffing-Cueni, D ; Kühn, L C ; Verrey, F</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c482t-3954a3dc692a5b9a7d4a8152676c91448668217f6db661ad28f2f6c40274de3e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Amino Acid Sequence</topic><topic>Amino Acid Transport Systems</topic><topic>Amino Acid Transport Systems, Basic</topic><topic>Amino Acids - metabolism</topic><topic>Animals</topic><topic>Biological Transport</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>Chromosomes, Human, Pair 19</topic><topic>Cloning, Molecular</topic><topic>Cystinuria - genetics</topic><topic>Cystinuria - metabolism</topic><topic>Fluorescent Antibody Technique</topic><topic>Humans</topic><topic>In Situ Hybridization</topic><topic>Kidney - metabolism</topic><topic>Kidney - ultrastructure</topic><topic>Male</topic><topic>Membrane Glycoproteins - genetics</topic><topic>Membrane Glycoproteins - metabolism</topic><topic>Mice</topic><topic>Microvilli - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Oocytes - metabolism</topic><topic>Organ Specificity</topic><topic>Sequence Alignment</topic><topic>Xenopus laevis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pfeiffer, R</creatorcontrib><creatorcontrib>Loffing, J</creatorcontrib><creatorcontrib>Rossier, G</creatorcontrib><creatorcontrib>Bauch, C</creatorcontrib><creatorcontrib>Meier, C</creatorcontrib><creatorcontrib>Eggermann, T</creatorcontrib><creatorcontrib>Loffing-Cueni, D</creatorcontrib><creatorcontrib>Kühn, L C</creatorcontrib><creatorcontrib>Verrey, F</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Molecular biology of the cell</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pfeiffer, R</au><au>Loffing, J</au><au>Rossier, G</au><au>Bauch, C</au><au>Meier, C</au><au>Eggermann, T</au><au>Loffing-Cueni, D</au><au>Kühn, L C</au><au>Verrey, F</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Luminal heterodimeric amino acid transporter defective in cystinuria</atitle><jtitle>Molecular biology of the cell</jtitle><addtitle>Mol Biol Cell</addtitle><date>1999-12-01</date><risdate>1999</risdate><volume>10</volume><issue>12</issue><spage>4135</spage><epage>4147</epage><pages>4135-4147</pages><issn>1059-1524</issn><eissn>1939-4586</eissn><abstract>Mutations of the glycoprotein rBAT cause cystinuria type I, an autosomal recessive failure of dibasic amino acid transport (b(0,+) type) across luminal membranes of intestine and kidney cells. Here we identify the permease-like protein b(0,+)AT as the catalytic subunit that associates by a disulfide bond with rBAT to form a hetero-oligomeric b(0,+) amino acid transporter complex. We demonstrate its b(0,+)-type amino acid transport kinetics using a heterodimeric fusion construct and show its luminal brush border localization in kidney proximal tubule. These biochemical, transport, and localization characteristics as well as the chromosomal localization on 19q support the notion that the b(0,+)AT protein is the product of the gene defective in non-type I cystinuria.</abstract><cop>United States</cop><pub>The American Society for Cell Biology</pub><pmid>10588648</pmid><doi>10.1091/mbc.10.12.4135</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Amino Acid Sequence Amino Acid Transport Systems Amino Acid Transport Systems, Basic Amino Acids - metabolism Animals Biological Transport Carrier Proteins - genetics Carrier Proteins - metabolism Chromosomes, Human, Pair 19 Cloning, Molecular Cystinuria - genetics Cystinuria - metabolism Fluorescent Antibody Technique Humans In Situ Hybridization Kidney - metabolism Kidney - ultrastructure Male Membrane Glycoproteins - genetics Membrane Glycoproteins - metabolism Mice Microvilli - metabolism Molecular Sequence Data Oocytes - metabolism Organ Specificity Sequence Alignment Xenopus laevis |
| title | Luminal heterodimeric amino acid transporter defective in cystinuria |
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