{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,2,7]],"date-time":"2026-02-07T16:25:49Z","timestamp":1770481549338,"version":"3.49.0"},"reference-count":85,"publisher":"The Company of Biologists","issue":"8","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":[],"published-print":{"date-parts":[[2009,4,15]]},"abstract":"<jats:p>Batten disease is characterised by lysosomal dysfunction. The most common type of the disease is caused by mutations in the membrane protein CLN3, whose function is unknown. We show that the fission yeast orthologue Btn1p, previously implicated in vacuole function, is required for correct sorting of the vacuole hydrolase carboxypeptidase Y (Cpy1p). This is, in part, due to a defect in trafficking of Vps10p, the sorting receptor for Cpy1p, from the Golgi to the trans-Golgi network in btn1\u0394 cells. Our data also implicate btn1 in other Vps10-independent Cpy1-sorting pathways. Furthermore, btn1 affects the number, intracellular location and structure of Golgi compartments. We show that the prevacuole location of Btn1p is at the Golgi, because Btn1p colocalises predominantly with the Golgi marker Gms1p in compartments that are sensitive to Brefeldin A. Btn1p function might be linked to that of Vps34p, a phosphatidylinositol 3-kinase, because Btn1p acts as a multicopy suppressor of the severe Cpy1p vacuole protein-sorting defect of vps34\u0394 cells. Together, these results indicate an important role for Btn1p in the Golgi complex, which affects Golgi homeostasis and vacuole protein sorting. We propose a similar role for CLN3 in mammalian cells.<\/jats:p>","DOI":"10.1242\/jcs.038323","type":"journal-article","created":{"date-parts":[[2009,3,20]],"date-time":"2009-03-20T00:33:34Z","timestamp":1237509214000},"page":"1163-1173","source":"Crossref","is-referenced-by-count":44,"title":["<i>S. pombe btn1<\/i>, the orthologue of the Batten disease gene<i>CLN3<\/i>, is required for vacuole protein sorting of Cpy1p and Golgi exit of Vps10p"],"prefix":"10.1242","volume":"122","author":[{"given":"Sandra","family":"Codlin","sequence":"first","affiliation":[{"name":"MRC Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Sara E.","family":"Mole","sequence":"additional","affiliation":[{"name":"MRC Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, UK"},{"name":"Molecular Medicine Unit, UCL Institute of Child Health, University College London, London WC1E 6BT, UK"},{"name":"Department of Genetics, Evolution and Environment, University College London, London WC1E 6BT, UK"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"237","reference":[{"key":"2021042521014800300_REF1","doi-asserted-by":"crossref","unstructured":"Andersen, O. 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L., Bilton, R. L., Woollatt, E., Chataway, T. K., Sutherland, G. R. and Callen, D. F. (1999). The Batten disease gene product (CLN3p) is a Golgi integral membrane protein. Hum. Mol. Genet.8, 523-531.","DOI":"10.1093\/hmg\/8.3.523"},{"key":"2021042521014800300_REF44","doi-asserted-by":"crossref","unstructured":"Kytta\u0308la\u0308, A., Ihrke, G., Vesa, J., Schell, M. J. and Luzio, J. P. (2004). Two motifs target Batten disease protein CLN3 to lysosomes in transfected non-neuronal and neuronal cells. Mol. Biol. Cell15, 1313-1323.","DOI":"10.1091\/mbc.e03-02-0120"},{"key":"2021042521014800300_REF45","doi-asserted-by":"crossref","unstructured":"Lawe, D. C., Patki, V., Heller-Harrison, R., Lambright, D. and Corvera, S. (2000). The FYVE domain of early endosome antigen 1 is required for both phosphatidylinositol 3-phosphate and Rab5 binding. Critical role of this dual interaction for endosomal localization. J. Biol. 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