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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 bioge...

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Autores principales: Golchoubian, Banafsheh, Brunner, Andreas, Bragulat-Teixidor, Helena, Neuner, Annett, Akarlar, Busra A., Ozlu, Nurhan, Schlaitz, Anne-Lore
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Rockefeller University Press 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8656412/
https://www.ncbi.nlm.nih.gov/pubmed/34874453
http://dx.doi.org/10.1083/jcb.202101049
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author Golchoubian, Banafsheh
Brunner, Andreas
Bragulat-Teixidor, Helena
Neuner, Annett
Akarlar, Busra A.
Ozlu, Nurhan
Schlaitz, Anne-Lore
author_facet Golchoubian, Banafsheh
Brunner, Andreas
Bragulat-Teixidor, Helena
Neuner, Annett
Akarlar, Busra A.
Ozlu, Nurhan
Schlaitz, Anne-Lore
author_sort Golchoubian, Banafsheh
collection PubMed
description 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.
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spelling pubmed-86564122022-07-14 Reticulon-like REEP4 at the inner nuclear membrane promotes nuclear pore complex formation Golchoubian, Banafsheh Brunner, Andreas Bragulat-Teixidor, Helena Neuner, Annett Akarlar, Busra A. Ozlu, Nurhan Schlaitz, Anne-Lore J Cell Biol Report 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. Rockefeller University Press 2021-12-07 /pmc/articles/PMC8656412/ /pubmed/34874453 http://dx.doi.org/10.1083/jcb.202101049 Text en © 2021 Golchoubian et al. https://creativecommons.org/licenses/by-nc-sa/4.0/http://www.rupress.org/terms/This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms/). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 International license, as described at https://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Report
Golchoubian, Banafsheh
Brunner, Andreas
Bragulat-Teixidor, Helena
Neuner, Annett
Akarlar, Busra A.
Ozlu, Nurhan
Schlaitz, Anne-Lore
Reticulon-like REEP4 at the inner nuclear membrane promotes nuclear pore complex formation
title Reticulon-like REEP4 at the inner nuclear membrane promotes nuclear pore complex formation
title_full Reticulon-like REEP4 at the inner nuclear membrane promotes nuclear pore complex formation
title_fullStr Reticulon-like REEP4 at the inner nuclear membrane promotes nuclear pore complex formation
title_full_unstemmed Reticulon-like REEP4 at the inner nuclear membrane promotes nuclear pore complex formation
title_short Reticulon-like REEP4 at the inner nuclear membrane promotes nuclear pore complex formation
title_sort reticulon-like reep4 at the inner nuclear membrane promotes nuclear pore complex formation
topic Report
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8656412/
https://www.ncbi.nlm.nih.gov/pubmed/34874453
http://dx.doi.org/10.1083/jcb.202101049
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