{"title":"α -突触核蛋白在内吞缺陷分裂酵母菌株中不能形成聚集体，∆myo1和∆end4。","authors":"Teruaki Takasaki, Ryuga Yamada, Yoshitaka Sugimoto, Reiko Sugiura","doi":"10.17912/micropub.biology.001479","DOIUrl":null,"url":null,"abstract":"<p><p>Alpha-Synuclein (α-Syn) is a soluble neuronal protein whose aggregation is one of the hallmarks of Parkinson's disease (PD). We previously developed a fission yeast model of PD that recapitulates α-Syn aggregation upon high-level expression of human α-Syn. Here, we show that α-Syn aggregate formation in yeast requires Myo1 and End4 , proteins essential for the early steps of endocytosis. α-Syn expression levels in Δ <i>myo1</i> and <i>∆end4</i> cells were comparable to wild-type cells, suggesting that defects in endocytosis disrupt α-Syn aggregation. These findings highlight the critical role of endocytosis in α-Syn aggregation and PD pathology.</p>","PeriodicalId":74192,"journal":{"name":"microPublication biology","volume":"2025 ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2025-01-21","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11795301/pdf/","citationCount":"0","resultStr":"{\"title\":\"Alpha-Synuclein Fails to Form Aggregates in Endocytosis-Defective Fission Yeast Strains, ∆ <i>myo1</i> and ∆ <i>end4</i>.\",\"authors\":\"Teruaki Takasaki, Ryuga Yamada, Yoshitaka Sugimoto, Reiko Sugiura\",\"doi\":\"10.17912/micropub.biology.001479\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Alpha-Synuclein (α-Syn) is a soluble neuronal protein whose aggregation is one of the hallmarks of Parkinson's disease (PD). We previously developed a fission yeast model of PD that recapitulates α-Syn aggregation upon high-level expression of human α-Syn. Here, we show that α-Syn aggregate formation in yeast requires Myo1 and End4 , proteins essential for the early steps of endocytosis. α-Syn expression levels in Δ <i>myo1</i> and <i>∆end4</i> cells were comparable to wild-type cells, suggesting that defects in endocytosis disrupt α-Syn aggregation. These findings highlight the critical role of endocytosis in α-Syn aggregation and PD pathology.</p>\",\"PeriodicalId\":74192,\"journal\":{\"name\":\"microPublication biology\",\"volume\":\"2025 \",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2025-01-21\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11795301/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"microPublication biology\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.17912/micropub.biology.001479\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2025/1/1 0:00:00\",\"PubModel\":\"eCollection\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"microPublication biology","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.17912/micropub.biology.001479","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2025/1/1 0:00:00","PubModel":"eCollection","JCR":"","JCRName":"","Score":null,"Total":0}
Alpha-Synuclein Fails to Form Aggregates in Endocytosis-Defective Fission Yeast Strains, ∆ myo1 and ∆ end4.
Alpha-Synuclein (α-Syn) is a soluble neuronal protein whose aggregation is one of the hallmarks of Parkinson's disease (PD). We previously developed a fission yeast model of PD that recapitulates α-Syn aggregation upon high-level expression of human α-Syn. Here, we show that α-Syn aggregate formation in yeast requires Myo1 and End4 , proteins essential for the early steps of endocytosis. α-Syn expression levels in Δ myo1 and ∆end4 cells were comparable to wild-type cells, suggesting that defects in endocytosis disrupt α-Syn aggregation. These findings highlight the critical role of endocytosis in α-Syn aggregation and PD pathology.
求助内容：
应助结果提醒方式：
京公网安备 11010802042870号
