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- W3194915460 abstract "Summary The integral membrane protein Apq12 is an important nuclear envelope (NE)/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 upon 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 during NPC biogenesis." @default.
- W3194915460 created "2021-08-30" @default.
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- W3194915460 date "2021-08-13" @default.
- W3194915460 modified "2023-09-26" @default.
- W3194915460 title "A short perinuclear amphipathic α-helix in Apq12 promotes nuclear pore complex biogenesis" @default.
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- W3194915460 doi "https://doi.org/10.1101/2021.08.13.456248" @default.
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