A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis

The integral membrane protein Apq12 is an important nuclear envelope (NE)/endoplasmic reticulum (ER) modulator that cooperates with the nuclear pore complex (NPC) biogenesis factors Brl1 and Brr6. How Apq12 executes these functions is unknown. Here, we identified a short amphipathic α-helix (AαH) in...

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Autores principales:	Wanlu Zhang, Azqa Khan, Jlenia Vitale, Annett Neuner, Kerstin Rink, Christian Lüchtenborg, Britta Brügger, Thomas H. Söllner, Elmar Schiebel
Formato:	article
Lenguaje:	EN
Publicado:	The Royal Society 2021
Materias:	APQ12 BRR6 nuclear pore complex nuclear envelope BRL1 nuclear pore complex biogenesis Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/49f2b3970e5e42359e25debff6fe7f98
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spelling	oai:doaj.org-article:49f2b3970e5e42359e25debff6fe7f982021-11-24T08:05:24ZA short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis10.1098/rsob.2102502046-2441https://doaj.org/article/49f2b3970e5e42359e25debff6fe7f982021-11-01T00:00:00Zhttps://royalsocietypublishing.org/doi/10.1098/rsob.210250https://doaj.org/toc/2046-2441The integral membrane protein Apq12 is an important nuclear envelope (NE)/endoplasmic reticulum (ER) modulator that cooperates with the nuclear pore complex (NPC) biogenesis factors Brl1 and Brr6. How Apq12 executes these functions is unknown. Here, we identified a short amphipathic α-helix (AαH) in Apq12 that links the two transmembrane domains in the perinuclear space and has liposome-binding properties. Cells expressing an APQ12 (apq12-ah) version in which AαH is disrupted show NPC biogenesis and NE integrity defects, without impacting Apq12-ah topology or NE/ER localization. Overexpression of APQ12 but not apq12-ah triggers striking over-proliferation of the outer nuclear membrane (ONM)/ER and promotes accumulation of phosphatidic acid (PA) at the NE. Apq12 and Apq12-ah both associate with NPC biogenesis intermediates and removal of AαH increases both Brl1 levels and the interaction between Brl1 and Brr6. We conclude that the short amphipathic α-helix of Apq12 regulates the function of Brl1 and Brr6 and promotes PA accumulation at the NE possibly during NPC biogenesis.Wanlu ZhangAzqa KhanJlenia VitaleAnnett NeunerKerstin RinkChristian LüchtenborgBritta BrüggerThomas H. SöllnerElmar SchiebelThe Royal SocietyarticleAPQ12BRR6nuclear pore complexnuclear envelopeBRL1nuclear pore complex biogenesisBiology (General)QH301-705.5ENOpen Biology, Vol 11, Iss 11 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	APQ12 BRR6 nuclear pore complex nuclear envelope BRL1 nuclear pore complex biogenesis Biology (General) QH301-705.5
spellingShingle	APQ12 BRR6 nuclear pore complex nuclear envelope BRL1 nuclear pore complex biogenesis Biology (General) QH301-705.5 Wanlu Zhang Azqa Khan Jlenia Vitale Annett Neuner Kerstin Rink Christian Lüchtenborg Britta Brügger Thomas H. Söllner Elmar Schiebel A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis
description	The integral membrane protein Apq12 is an important nuclear envelope (NE)/endoplasmic reticulum (ER) modulator that cooperates with the nuclear pore complex (NPC) biogenesis factors Brl1 and Brr6. How Apq12 executes these functions is unknown. Here, we identified a short amphipathic α-helix (AαH) in Apq12 that links the two transmembrane domains in the perinuclear space and has liposome-binding properties. Cells expressing an APQ12 (apq12-ah) version in which AαH is disrupted show NPC biogenesis and NE integrity defects, without impacting Apq12-ah topology or NE/ER localization. Overexpression of APQ12 but not apq12-ah triggers striking over-proliferation of the outer nuclear membrane (ONM)/ER and promotes accumulation of phosphatidic acid (PA) at the NE. Apq12 and Apq12-ah both associate with NPC biogenesis intermediates and removal of AαH increases both Brl1 levels and the interaction between Brl1 and Brr6. We conclude that the short amphipathic α-helix of Apq12 regulates the function of Brl1 and Brr6 and promotes PA accumulation at the NE possibly during NPC biogenesis.
format	article
author	Wanlu Zhang Azqa Khan Jlenia Vitale Annett Neuner Kerstin Rink Christian Lüchtenborg Britta Brügger Thomas H. Söllner Elmar Schiebel
author_facet	Wanlu Zhang Azqa Khan Jlenia Vitale Annett Neuner Kerstin Rink Christian Lüchtenborg Britta Brügger Thomas H. Söllner Elmar Schiebel
author_sort	Wanlu Zhang
title	A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis
title_short	A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis
title_full	A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis
title_fullStr	A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis
title_full_unstemmed	A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis
title_sort	short perinuclear amphipathic α-helix in apq12 promotes nuclear pore complex biogenesis
publisher	The Royal Society
publishDate	2021
url	https://doaj.org/article/49f2b3970e5e42359e25debff6fe7f98
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A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis

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