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胞吐质膜流重塑内质网-质膜连接，以组装隔丝套环。

Exocytic plasma membrane flows remodel endoplasmic reticulum-plasma membrane tethering for septin collar assembly.

机构信息

Okinawa Institute of Science and Technology Graduate University, 1919-1 Tancha, Onna, Okinawa 904-0495, Japan.

出版信息

Sci Adv. 2024 Mar 15;10(11):eadj1512. doi: 10.1126/sciadv.adj1512. Epub 2024 Mar 13.

DOI:10.1126/sciadv.adj1512
PMID:38478607
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10936878/
Abstract

Endoplasmic reticulum (ER)-plasma membrane (PM) tethering is crucial for the non-vesicular lipid transport between the ER membrane and the PM. However, the PM-associated ER can impede the PM binding of cytoskeletons and other organelles. It is poorly understood how the competition between the ER and cytoskeletons/organelles on the PM is resolved. Here, we show that, upon septin collar assembly, ER-PM tethering proteins are excluded from the yeast bud sites, and the PM-associated ER is locally detached from the PM. Our results suggest that PM flows by polarized exocytosis extrude PM proteins, including ER-PM tethering proteins, from the bud sites. When the reorganization of the ER-PM tethering was inhibited by exocytosis repression, septin localization was restricted to the PM sites poor in ER-PM tethering proteins. This study proposes machinery reconciling ER-septin competition on the PM, providing mechanistic insights into the spatial organization of PM-associated organelles and cytoskeletons.

摘要

内质网（ER）-质膜（PM）连接对于 ER 膜和 PM 之间的非囊泡脂质转运至关重要。然而，PM 相关的 ER 会阻碍 PM 与细胞骨架和其他细胞器的结合。目前尚不清楚 ER 和 PM 上的细胞骨架/细胞器之间的竞争是如何解决的。在这里，我们表明，在 septin 套环组装后，ER-PM 连接蛋白被排除在酵母芽位点之外，并且 PM 相关的 ER 从 PM 上局部脱离。我们的结果表明，通过极化胞吐作用，PM 流将 PM 蛋白（包括 ER-PM 连接蛋白）从芽位点挤出。当通过抑制胞吐作用来抑制 ER-PM 连接的重排时，septin 定位被限制在 ER-PM 连接蛋白含量低的 PM 位点。这项研究提出了一种协调 PM 上 ER-septin 竞争的机制，为 PM 相关细胞器和细胞骨架的空间组织提供了机制上的见解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48ae/10936878/48fd5a9e5de5/sciadv.adj1512-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48ae/10936878/1ad2419bb1b7/sciadv.adj1512-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48ae/10936878/238eca3988f1/sciadv.adj1512-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48ae/10936878/72b1c46764c1/sciadv.adj1512-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48ae/10936878/6b7eb6028e1d/sciadv.adj1512-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48ae/10936878/7413ccd50c3a/sciadv.adj1512-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48ae/10936878/48fd5a9e5de5/sciadv.adj1512-f6.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48ae/10936878/1ad2419bb1b7/sciadv.adj1512-f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48ae/10936878/238eca3988f1/sciadv.adj1512-f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48ae/10936878/72b1c46764c1/sciadv.adj1512-f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48ae/10936878/6b7eb6028e1d/sciadv.adj1512-f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48ae/10936878/7413ccd50c3a/sciadv.adj1512-f5.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/48ae/10936878/48fd5a9e5de5/sciadv.adj1512-f6.jpg

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