TFG regulates inner COPII coat recruitment to facilitate anterograde secretory protein transport.

IF 4.3 3区 材料科学 Q1 ENGINEERING, ELECTRICAL & ELECTRONIC
ACS Applied Electronic Materials Pub Date : 2024-08-01 Epub Date: 2024-07-10 DOI:10.1091/mbc.E24-06-0282
William Kasberg, Peter Luong, Kayla Minushkin, Iryna Pustova, Kevin A Swift, Meixian Zhao, Anjon Audhya
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引用次数: 0

Abstract

Coat protein complex II (COPII) governs the initial steps of biosynthetic secretory protein transport from the endoplasmic reticulum (ER), facilitating the movement of a wide variety of cargoes. Here, we demonstrate that Trk-fused gene (TFG) regulates the rate at which inner COPII coat proteins are concentrated at ER subdomains. Specifically, in cells lacking TFG, the GTPase-activating protein (GAP) Sec23 accumulates more rapidly at budding sites on the ER as compared with control cells, potentially altering the normal timing of GTP hydrolysis on Sar1. Under these conditions, anterograde trafficking of several secretory cargoes is delayed, irrespective of their predicted size. We propose that TFG controls the local, freely available pool of Sec23 during COPII coat formation and limits its capacity to prematurely destabilize COPII complexes on the ER. This function of TFG enables it to act akin to a rheostat, promoting the ordered recruitment of Sec23, which is critical for efficient secretory cargo export.

TFG 可调节 COPII 内膜的募集,从而促进分泌蛋白的前向运输。
衣壳蛋白复合体 II(COPII)控制着生物合成分泌蛋白从内质网(ER)转运的最初步骤,促进了各种货物的移动。在这里,我们证明了 Trk 融合基因(TFG)能调节内 COPII 外壳蛋白在 ER 亚域集中的速度。具体来说,与对照细胞相比,在缺乏 TFG 的细胞中,GTP 酶激活蛋白(GAP)Sec23 在 ER 上的出芽点积累得更快,这可能会改变 Sar1 上 GTP 水解的正常时间。在这些条件下,几种分泌货物的前向运输被延迟,无论其预测大小如何。我们认为,在 COPII 涂层形成过程中,TFG 控制着 Sec23 的局部自由可用池,并限制其过早地破坏 ER 上 COPII 复合物稳定性的能力。TFG 的这一功能使其能够发挥类似于流变调节器的作用,促进 Sec23 的有序招募,这对分泌货物的高效输出至关重要。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
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来源期刊
CiteScore
7.20
自引率
4.30%
发文量
567
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