{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T02:12:52Z","timestamp":1791252772231,"version":"4.1.0"},"reference-count":43,"publisher":"American Association for the Advancement of Science (AAAS)","issue":"6092","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Science"],"published-print":{"date-parts":[[2012,7,20]]},"abstract":"<jats:title>Lysosomal Amino Acid Transporter<\/jats:title>\n                  <jats:p>\n                    Cystinosis is characterized by intralysosomal accumulation of free cystine, which results in age-dependent problems in the kidney, muscle, retina, and central nervous system. The disease-causing gene encodes a lysosomal cystine transporter. The most effective therapeutic agent for cystinosis, cysteamine, depletes lysosomal free cystine by converting it to cysteine and the mixed disulfide cysteine-cysteamine, which can then be exported from lysosomes as a lysine analog through a putative lysine\/cationic amino acid transporter. Using an unbiased genetic screen for\n                    <jats:italic>Caenorhabditis elegans<\/jats:italic>\n                    mutants with increased accumulation of apoptotic cells or autophagosomes,\n                    <jats:bold>\n                      Liu\n                      <jats:italic>et al.<\/jats:italic>\n                    <\/jats:bold>\n                    (p.\n                    <jats:related-article xmlns:xlink=\"http:\/\/www.w3.org\/1999\/xlink\" ext-link-type=\"doi\" page=\"351\" related-article-type=\"in-this-issue\" vol=\"337\" xlink:href=\"10.1126\/science.1220281\">351<\/jats:related-article>\n                    ) now reveal the molecular identity of a lysosomal lysine\/arginine transporter that plays a role in maintaining lysosome function and amino acid homeostasis and that can explain how cysteamine alleviates a lysosomal storage disease.\n                  <\/jats:p>","DOI":"10.1126\/science.1220281","type":"journal-article","created":{"date-parts":[[2012,7,19]],"date-time":"2012-07-19T18:44:24Z","timestamp":1342723464000},"page":"351-354","source":"Crossref","is-referenced-by-count":199,"title":["LAAT-1 Is the Lysosomal Lysine\/Arginine Transporter That Maintains Amino Acid Homeostasis"],"prefix":"10.1126","volume":"337","author":[{"given":"Bin","family":"Liu","sequence":"first","affiliation":[{"name":"Graduate Program in Chinese Academy of Medical Sciences and Peking Union Medical College, China."},{"name":"National Institute of Biological Sciences, No. 7 Science Park Road, Zhongguancun Life Science Park, Beijing 102206, China."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hongwei","family":"Du","sequence":"additional","affiliation":[{"name":"State Key Laboratory of Molecular and Developmental Biology, Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China."},{"name":"Graduate School, Chinese Academy of Sciences, Beijing 100039, China."},{"name":"National Institute of Biological Sciences, No. 7 Science Park Road, Zhongguancun Life Science Park, Beijing 102206, China."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Rachael","family":"Rutkowski","sequence":"additional","affiliation":[{"name":"Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anton","family":"Gartner","sequence":"additional","affiliation":[{"name":"Wellcome Trust Centre for Gene Regulation and Expression, College of Life Sciences, University of Dundee, Dundee DD1 5EH, UK."}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiaochen","family":"Wang","sequence":"additional","affiliation":[{"name":"National Institute of Biological Sciences, No. 7 Science Park Road, Zhongguancun Life Science Park, Beijing 102206, China."}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"221","reference":[{"key":"e_1_3_2_2_2","doi-asserted-by":"publisher","DOI":"10.1007\/s10545-008-0879-9"},{"key":"e_1_3_2_3_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.7112129"},{"key":"e_1_3_2_4_2","doi-asserted-by":"publisher","DOI":"10.1073\/pnas.79.14.4442"},{"key":"e_1_3_2_5_2","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/20.21.5940"},{"key":"e_1_3_2_6_2","doi-asserted-by":"publisher","DOI":"10.1172\/JCI108448"},{"key":"e_1_3_2_7_2","doi-asserted-by":"crossref","first-page":"545","DOI":"10.1042\/bj2280545","article-title":"Cysteamine depletes cystinotic leucocyte granular fractions of cystine by the mechanism of disulphide interchange","volume":"228","author":"Gahl W. 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