{"title":"ESCRT复合物:膜转运网络的结构和机制。","authors":"James H Hurley, Scott D Emr","doi":"10.1146/annurev.biophys.35.040405.102126","DOIUrl":null,"url":null,"abstract":"<p><p>The ESCRT complexes and associated proteins comprise a major pathway for the lysosomal degradation of transmembrane proteins and are critical for receptor downregulation, budding of the HIV virus, and other normal and pathological cell processes. The ESCRT system is conserved from yeast to humans. The ESCRT complexes form a network that recruits monoubiquitinated proteins and drives their internalization into lumenal vesicles within a type of endosome known as a multivesicular body. The structures and interactions of many of the components have been determined over the past three years, revealing mechanisms for membrane and cargo recruitment and for complex assembly.</p>","PeriodicalId":8270,"journal":{"name":"Annual review of biophysics and biomolecular structure","volume":"35 ","pages":"277-98"},"PeriodicalIF":0.0000,"publicationDate":"2006-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1146/annurev.biophys.35.040405.102126","citationCount":"556","resultStr":"{\"title\":\"The ESCRT complexes: structure and mechanism of a membrane-trafficking network.\",\"authors\":\"James H Hurley, Scott D Emr\",\"doi\":\"10.1146/annurev.biophys.35.040405.102126\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>The ESCRT complexes and associated proteins comprise a major pathway for the lysosomal degradation of transmembrane proteins and are critical for receptor downregulation, budding of the HIV virus, and other normal and pathological cell processes. The ESCRT system is conserved from yeast to humans. The ESCRT complexes form a network that recruits monoubiquitinated proteins and drives their internalization into lumenal vesicles within a type of endosome known as a multivesicular body. The structures and interactions of many of the components have been determined over the past three years, revealing mechanisms for membrane and cargo recruitment and for complex assembly.</p>\",\"PeriodicalId\":8270,\"journal\":{\"name\":\"Annual review of biophysics and biomolecular structure\",\"volume\":\"35 \",\"pages\":\"277-98\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2006-01-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1146/annurev.biophys.35.040405.102126\",\"citationCount\":\"556\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Annual review of biophysics and biomolecular structure\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1146/annurev.biophys.35.040405.102126\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Annual review of biophysics and biomolecular structure","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1146/annurev.biophys.35.040405.102126","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"","JCRName":"","Score":null,"Total":0}
The ESCRT complexes: structure and mechanism of a membrane-trafficking network.
The ESCRT complexes and associated proteins comprise a major pathway for the lysosomal degradation of transmembrane proteins and are critical for receptor downregulation, budding of the HIV virus, and other normal and pathological cell processes. The ESCRT system is conserved from yeast to humans. The ESCRT complexes form a network that recruits monoubiquitinated proteins and drives their internalization into lumenal vesicles within a type of endosome known as a multivesicular body. The structures and interactions of many of the components have been determined over the past three years, revealing mechanisms for membrane and cargo recruitment and for complex assembly.