{"title":"CLN3结合溶酶体清除甘油磷脂","authors":"Guang Lu, Han-Ming Shen","doi":"10.1093/lifemeta/loac029","DOIUrl":null,"url":null,"abstract":"\n CLN3 is a lysosomal transmembrane protein and loss of CLN3 mutation is known to cause a juvenile lethal neurodegenerative lysosomal storage disorder (LSD), called Batten disease. In a recent study published in Nature, Laqtom et al. reported a novel function of CLN3 in the clearance of glycerophospholipid from lysosomes via lysosomal efflux of glycerophosphodiesters (GPDs), not only establishing a deeper mechanistic understanding of Batten disease, also suggesting both the diagnostic and therapeutic potential of CLN3-GPDs in this type of neurodegenerative LSD.","PeriodicalId":74074,"journal":{"name":"Life metabolism","volume":null,"pages":null},"PeriodicalIF":0.0000,"publicationDate":"2022-10-19","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"CLN3 clinches lysosomes in clearance of glycerophospholipids\",\"authors\":\"Guang Lu, Han-Ming Shen\",\"doi\":\"10.1093/lifemeta/loac029\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"\\n CLN3 is a lysosomal transmembrane protein and loss of CLN3 mutation is known to cause a juvenile lethal neurodegenerative lysosomal storage disorder (LSD), called Batten disease. In a recent study published in Nature, Laqtom et al. reported a novel function of CLN3 in the clearance of glycerophospholipid from lysosomes via lysosomal efflux of glycerophosphodiesters (GPDs), not only establishing a deeper mechanistic understanding of Batten disease, also suggesting both the diagnostic and therapeutic potential of CLN3-GPDs in this type of neurodegenerative LSD.\",\"PeriodicalId\":74074,\"journal\":{\"name\":\"Life metabolism\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2022-10-19\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Life metabolism\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1093/lifemeta/loac029\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Life metabolism","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1093/lifemeta/loac029","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
CLN3 clinches lysosomes in clearance of glycerophospholipids
CLN3 is a lysosomal transmembrane protein and loss of CLN3 mutation is known to cause a juvenile lethal neurodegenerative lysosomal storage disorder (LSD), called Batten disease. In a recent study published in Nature, Laqtom et al. reported a novel function of CLN3 in the clearance of glycerophospholipid from lysosomes via lysosomal efflux of glycerophosphodiesters (GPDs), not only establishing a deeper mechanistic understanding of Batten disease, also suggesting both the diagnostic and therapeutic potential of CLN3-GPDs in this type of neurodegenerative LSD.