内膜上网状的REEP4促进核孔复合物的形成。

The Journal of Cell Biology Pub Date : 2022-02-07 Epub Date: 2021-12-07 DOI:10.1083/jcb.202101049
Banafsheh Golchoubian, Andreas Brunner, Helena Bragulat-Teixidor, Annett Neuner, Busra A Akarlar, Nurhan Ozlu, Anne-Lore Schlaitz
{"title":"内膜上网状的REEP4促进核孔复合物的形成。","authors":"Banafsheh Golchoubian,&nbsp;Andreas Brunner,&nbsp;Helena Bragulat-Teixidor,&nbsp;Annett Neuner,&nbsp;Busra A Akarlar,&nbsp;Nurhan Ozlu,&nbsp;Anne-Lore Schlaitz","doi":"10.1083/jcb.202101049","DOIUrl":null,"url":null,"abstract":"<p><p>Nuclear pore complexes (NPCs) are channels within the nuclear envelope that mediate nucleocytoplasmic transport. NPCs form within the closed nuclear envelope during interphase or assemble concomitantly with nuclear envelope reformation in late stages of mitosis. Both interphase and mitotic NPC biogenesis require coordination of protein complex assembly and membrane deformation. During early stages of mitotic NPC assembly, a seed for new NPCs is established on chromatin, yet the factors connecting the NPC seed to the membrane of the forming nuclear envelope are unknown. Here, we report that the reticulon homology domain protein REEP4 not only localizes to high-curvature membrane of the cytoplasmic endoplasmic reticulum but is also recruited to the inner nuclear membrane by the NPC biogenesis factor ELYS. This ELYS-recruited pool of REEP4 promotes NPC assembly and appears to be particularly important for NPC formation during mitosis. These findings suggest a role for REEP4 in coordinating nuclear envelope reformation with mitotic NPC biogenesis.</p>","PeriodicalId":343306,"journal":{"name":"The Journal of Cell Biology","volume":" ","pages":""},"PeriodicalIF":0.0000,"publicationDate":"2022-02-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/5d/c1/JCB_202101049.PMC8656412.pdf","citationCount":"6","resultStr":"{\"title\":\"Reticulon-like REEP4 at the inner nuclear membrane promotes nuclear pore complex formation.\",\"authors\":\"Banafsheh Golchoubian,&nbsp;Andreas Brunner,&nbsp;Helena Bragulat-Teixidor,&nbsp;Annett Neuner,&nbsp;Busra A Akarlar,&nbsp;Nurhan Ozlu,&nbsp;Anne-Lore Schlaitz\",\"doi\":\"10.1083/jcb.202101049\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>Nuclear pore complexes (NPCs) are channels within the nuclear envelope that mediate nucleocytoplasmic transport. NPCs form within the closed nuclear envelope during interphase or assemble concomitantly with nuclear envelope reformation in late stages of mitosis. Both interphase and mitotic NPC biogenesis require coordination of protein complex assembly and membrane deformation. During early stages of mitotic NPC assembly, a seed for new NPCs is established on chromatin, yet the factors connecting the NPC seed to the membrane of the forming nuclear envelope are unknown. Here, we report that the reticulon homology domain protein REEP4 not only localizes to high-curvature membrane of the cytoplasmic endoplasmic reticulum but is also recruited to the inner nuclear membrane by the NPC biogenesis factor ELYS. This ELYS-recruited pool of REEP4 promotes NPC assembly and appears to be particularly important for NPC formation during mitosis. These findings suggest a role for REEP4 in coordinating nuclear envelope reformation with mitotic NPC biogenesis.</p>\",\"PeriodicalId\":343306,\"journal\":{\"name\":\"The Journal of Cell Biology\",\"volume\":\" \",\"pages\":\"\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2022-02-07\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/5d/c1/JCB_202101049.PMC8656412.pdf\",\"citationCount\":\"6\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"The Journal of Cell Biology\",\"FirstCategoryId\":\"99\",\"ListUrlMain\":\"https://doi.org/10.1083/jcb.202101049\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2021/12/7 0:00:00\",\"PubModel\":\"Epub\",\"JCR\":\"\",\"JCRName\":\"\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"The Journal of Cell Biology","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1083/jcb.202101049","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2021/12/7 0:00:00","PubModel":"Epub","JCR":"","JCRName":"","Score":null,"Total":0}
引用次数: 6

摘要

核孔复合物(NPCs)是核膜内介导核胞质运输的通道。在有丝分裂后期,npc在封闭的核包膜内形成或与核包膜重组一起聚集。间期和有丝分裂鼻咽癌的生物发生都需要蛋白质复合物的组装和膜变形的协调。在有丝分裂NPC组装的早期阶段,新的NPC种子在染色质上建立,然而连接NPC种子与形成核膜的膜的因素是未知的。在这里,我们报道了网状同源结构域蛋白REEP4不仅定位于细胞质内质网的高曲率膜,而且还被NPC生物发生因子ELYS募集到核膜。这个由elys募集的REEP4库促进NPC的组装,似乎对有丝分裂期间NPC的形成特别重要。这些发现提示REEP4在协调核包膜重组和有丝分裂NPC生物发生中起着重要作用。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Reticulon-like REEP4 at the inner nuclear membrane promotes nuclear pore complex formation.

Nuclear pore complexes (NPCs) are channels within the nuclear envelope that mediate nucleocytoplasmic transport. NPCs form within the closed nuclear envelope during interphase or assemble concomitantly with nuclear envelope reformation in late stages of mitosis. Both interphase and mitotic NPC biogenesis require coordination of protein complex assembly and membrane deformation. During early stages of mitotic NPC assembly, a seed for new NPCs is established on chromatin, yet the factors connecting the NPC seed to the membrane of the forming nuclear envelope are unknown. Here, we report that the reticulon homology domain protein REEP4 not only localizes to high-curvature membrane of the cytoplasmic endoplasmic reticulum but is also recruited to the inner nuclear membrane by the NPC biogenesis factor ELYS. This ELYS-recruited pool of REEP4 promotes NPC assembly and appears to be particularly important for NPC formation during mitosis. These findings suggest a role for REEP4 in coordinating nuclear envelope reformation with mitotic NPC biogenesis.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
自引率
0.00%
发文量
0
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信