Coronin 1C restricts endosomal branched actin to organize ER contact and endosome fission.

The Journal of Cell Biology Pub Date : 2022-08-01 Epub Date: 2022-07-08 DOI:10.1083/jcb.202110089
Jonathan F Striepen, Gia K Voeltz
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引用次数: 7

Abstract

ER contact sites define the position of endosome bud fission during actin-dependent cargo sorting. Disrupting endosomal actin structures prevents retrograde cargo movement; however, how actin affects ER contact site formation and endosome fission is not known. Here we show that in contrast with the WASH complex, actin, its nucleator ARP2/3, and COR1C form a contained structure at the bud neck that defines the site of bud fission. We found that actin confinement is facilitated by type I coronins. Depletion of type I coronins allows actin to extend along the length of the bud in an ARP2/3-dependent manner. We demonstrate that extension of branched actin prevents ER recruitment and stalls buds before fission. Finally, our structure-function studies show that the COR1C's coiled-coil domain is sufficient to restore actin confinement, ER recruitment, and endosome fission. Together, our data reveal how the dynamics of endosomal actin and activity of actin regulators organize ER-associated bud fission.

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冠状蛋白1C限制核内体分支肌动蛋白组织内质网接触和核内体裂变。
内质网接触位点决定了在肌动蛋白依赖的货物分拣过程中核内体芽裂变的位置。破坏内体肌动蛋白结构可防止货物逆行运动;然而,肌动蛋白如何影响内质网接触位点形成和核内体裂变尚不清楚。与WASH复合物不同,肌动蛋白及其成核子ARP2/3和COR1C在芽颈处形成一个包含结构,定义了芽裂变的位置。我们发现I型冠状蛋白促进了肌动蛋白的约束。I型冠状蛋白的耗尽允许肌动蛋白以依赖arp2 /3的方式沿着芽的长度延伸。我们证明了分支肌动蛋白的延伸阻止了内质网的招募,并在分裂前阻止了芽的生长。最后,我们的结构-功能研究表明,COR1C的卷曲-卷曲结构域足以恢复肌动蛋白约束、内质网募集和核内体裂变。总之,我们的数据揭示了内体肌动蛋白的动力学和肌动蛋白调节因子的活性如何组织内质网相关的芽裂变。
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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