{"title":"核出口受体CRM1/XPO1及其各种货物。","authors":"Ralph H Kehlenbach, Yuh Min Chook","doi":"10.1016/j.tibs.2025.09.003","DOIUrl":null,"url":null,"abstract":"<p><p>CRM1 (Exportin 1, XPO1), the best-characterized nuclear export receptor, exports hundreds of proteins and various RNA species. Its broad cargo repertoire necessitates versatile binding modes for diverse interaction partners, including nuclear export signal/sequence (NES)-containing cargoes, the GTPase Ran, nucleoporins that line nuclear pore complexes, and accessory proteins that facilitate export complex assembly or disassembly. We review the current knowledge of CRM1's protein and RNA cargoes and examine its modes of interactions in the context of the basic mechanism of nuclear export - NES recognition, recent structural studies that reveal how CRM1 engages cargoes beyond NESs, and allosteric regulation. Finally, we touch on the state of NES/cargo prediction, CRM1's interactions with nucleoporins, and its emerging roles beyond nuclear export.</p>","PeriodicalId":440,"journal":{"name":"Trends in Biochemical Sciences","volume":" ","pages":""},"PeriodicalIF":11.0000,"publicationDate":"2025-09-27","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"The nuclear export receptor CRM1/XPO1 and its diverse cargoes.\",\"authors\":\"Ralph H Kehlenbach, Yuh Min Chook\",\"doi\":\"10.1016/j.tibs.2025.09.003\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>CRM1 (Exportin 1, XPO1), the best-characterized nuclear export receptor, exports hundreds of proteins and various RNA species. Its broad cargo repertoire necessitates versatile binding modes for diverse interaction partners, including nuclear export signal/sequence (NES)-containing cargoes, the GTPase Ran, nucleoporins that line nuclear pore complexes, and accessory proteins that facilitate export complex assembly or disassembly. We review the current knowledge of CRM1's protein and RNA cargoes and examine its modes of interactions in the context of the basic mechanism of nuclear export - NES recognition, recent structural studies that reveal how CRM1 engages cargoes beyond NESs, and allosteric regulation. Finally, we touch on the state of NES/cargo prediction, CRM1's interactions with nucleoporins, and its emerging roles beyond nuclear export.</p>\",\"PeriodicalId\":440,\"journal\":{\"name\":\"Trends in Biochemical Sciences\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":11.0000,\"publicationDate\":\"2025-09-27\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Trends in Biochemical Sciences\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1016/j.tibs.2025.09.003\",\"RegionNum\":1,\"RegionCategory\":\"生物学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"BIOCHEMISTRY & MOLECULAR BIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Trends in Biochemical Sciences","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1016/j.tibs.2025.09.003","RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
The nuclear export receptor CRM1/XPO1 and its diverse cargoes.
CRM1 (Exportin 1, XPO1), the best-characterized nuclear export receptor, exports hundreds of proteins and various RNA species. Its broad cargo repertoire necessitates versatile binding modes for diverse interaction partners, including nuclear export signal/sequence (NES)-containing cargoes, the GTPase Ran, nucleoporins that line nuclear pore complexes, and accessory proteins that facilitate export complex assembly or disassembly. We review the current knowledge of CRM1's protein and RNA cargoes and examine its modes of interactions in the context of the basic mechanism of nuclear export - NES recognition, recent structural studies that reveal how CRM1 engages cargoes beyond NESs, and allosteric regulation. Finally, we touch on the state of NES/cargo prediction, CRM1's interactions with nucleoporins, and its emerging roles beyond nuclear export.
期刊介绍：
For over 40 years, Trends in Biochemical Sciences (TIBS) has been a leading publication keeping readers informed about recent advances in all areas of biochemistry and molecular biology. Through monthly, peer-reviewed issues, TIBS covers a wide range of topics, from traditional subjects like protein structure and function to emerging areas in signaling and metabolism. Articles are curated by the Editor and authored by top researchers in their fields, with a focus on moving beyond simple literature summaries to providing novel insights and perspectives. Each issue primarily features concise and timely Reviews and Opinions, supplemented by shorter articles including Spotlights, Forums, and Technology of the Month, as well as impactful pieces like Science & Society and Scientific Life articles.
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