The function of the inner nuclear envelope protein SUN1 in mRNA export is regulated by phosphorylation

Abstract SUN1, a component of the LINC (Linker of Nucleoskeleton and Cytoskeleton) complex, functions in mammalian mRNA export through the NXF1-dependent pathway. It associates with mRNP complexes by direct interaction with NXF1. It also binds to the NPC through association with the nuclear pore com...

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Autores principales:	Ping Li, Maria Stumpf, Rolf Müller, Ludwig Eichinger, Gernot Glöckner, Angelika A. Noegel
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2017
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/d2506abca7434767a8c176879e184827
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spelling	oai:doaj.org-article:d2506abca7434767a8c176879e1848272021-12-02T15:05:35ZThe function of the inner nuclear envelope protein SUN1 in mRNA export is regulated by phosphorylation10.1038/s41598-017-08837-72045-2322https://doaj.org/article/d2506abca7434767a8c176879e1848272017-08-01T00:00:00Zhttps://doi.org/10.1038/s41598-017-08837-7https://doaj.org/toc/2045-2322Abstract SUN1, a component of the LINC (Linker of Nucleoskeleton and Cytoskeleton) complex, functions in mammalian mRNA export through the NXF1-dependent pathway. It associates with mRNP complexes by direct interaction with NXF1. It also binds to the NPC through association with the nuclear pore component Nup153, which is involved in mRNA export. The SUN1-NXF1 association is at least partly regulated by a protein kinase C (PKC) which phosphorylates serine 113 (S113) in the N-terminal domain leading to reduced interaction. The phosphorylation appears to be important for the SUN1 function in nuclear mRNA export since GFP-SUN1 carrying a S113A mutation was less efficient in restoring mRNA export after SUN1 knockdown as compared to the wild type protein. By contrast, GFP-SUN1-S113D resembling the phosphorylated state allowed very efficient export of poly(A)+RNA. Furthermore, probing a possible role of the LINC complex component Nesprin-2 in this process we observed impaired mRNA export in Nesprin-2 knockdown cells. This effect might be independent of SUN1 as expression of a GFP tagged SUN-domain deficient SUN1, which no longer can interact with Nesprin-2, did not affect mRNA export.Ping LiMaria StumpfRolf MüllerLudwig EichingerGernot GlöcknerAngelika A. NoegelNature PortfolioarticleMedicineRScienceQENScientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Ping Li Maria Stumpf Rolf Müller Ludwig Eichinger Gernot Glöckner Angelika A. Noegel The function of the inner nuclear envelope protein SUN1 in mRNA export is regulated by phosphorylation
description	Abstract SUN1, a component of the LINC (Linker of Nucleoskeleton and Cytoskeleton) complex, functions in mammalian mRNA export through the NXF1-dependent pathway. It associates with mRNP complexes by direct interaction with NXF1. It also binds to the NPC through association with the nuclear pore component Nup153, which is involved in mRNA export. The SUN1-NXF1 association is at least partly regulated by a protein kinase C (PKC) which phosphorylates serine 113 (S113) in the N-terminal domain leading to reduced interaction. The phosphorylation appears to be important for the SUN1 function in nuclear mRNA export since GFP-SUN1 carrying a S113A mutation was less efficient in restoring mRNA export after SUN1 knockdown as compared to the wild type protein. By contrast, GFP-SUN1-S113D resembling the phosphorylated state allowed very efficient export of poly(A)+RNA. Furthermore, probing a possible role of the LINC complex component Nesprin-2 in this process we observed impaired mRNA export in Nesprin-2 knockdown cells. This effect might be independent of SUN1 as expression of a GFP tagged SUN-domain deficient SUN1, which no longer can interact with Nesprin-2, did not affect mRNA export.
format	article
author	Ping Li Maria Stumpf Rolf Müller Ludwig Eichinger Gernot Glöckner Angelika A. Noegel
author_facet	Ping Li Maria Stumpf Rolf Müller Ludwig Eichinger Gernot Glöckner Angelika A. Noegel
author_sort	Ping Li
title	The function of the inner nuclear envelope protein SUN1 in mRNA export is regulated by phosphorylation
title_short	The function of the inner nuclear envelope protein SUN1 in mRNA export is regulated by phosphorylation
title_full	The function of the inner nuclear envelope protein SUN1 in mRNA export is regulated by phosphorylation
title_fullStr	The function of the inner nuclear envelope protein SUN1 in mRNA export is regulated by phosphorylation
title_full_unstemmed	The function of the inner nuclear envelope protein SUN1 in mRNA export is regulated by phosphorylation
title_sort	function of the inner nuclear envelope protein sun1 in mrna export is regulated by phosphorylation
publisher	Nature Portfolio
publishDate	2017
url	https://doaj.org/article/d2506abca7434767a8c176879e184827
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The function of the inner nuclear envelope protein SUN1 in mRNA export is regulated by phosphorylation

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