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核糖体组装因子 LSG1 与囊泡相关膜蛋白相关蛋白(VAPs)相互作用。

The Ribosome Assembly Factor LSG1 Interacts with Vesicle-Associated Membrane Protein-Associated Proteins (VAPs).

机构信息

Interdisciplinary Life Sciences Graduate Program, The University of Texas at Austin, Austin, Texas, USA.

Department of Molecular Biosciences, The University of Texas at Austin, Austin, Texas, USA.

出版信息

Mol Cell Biol. 2024;44(9):345-357. doi: 10.1080/10985549.2024.2384600. Epub 2024 Aug 12.

DOI:10.1080/10985549.2024.2384600
PMID:39133101
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC11376406/
Abstract

LSG1 is a conserved GTPase involved in ribosome assembly. It is required for the eviction of the nuclear export adapter NMD3 from the pre-60S subunit in the cytoplasm. In human cells, LSG1 has also been shown to interact with vesicle-associated membrane protein-associated proteins (VAPs) that are found primarily on the endoplasmic reticulum. VAPs interact with a large host of proteins which contain FFAT motifs (two phenylalanines (FF) in an acidic tract) and are involved in many cellular functions including membrane traffic and regulation of lipid transport. Here, we show that human LSG1 binds to VAPs via a noncanonical FFAT-like motif. Deletion of this motif specifically disrupts the localization of LSG1 to the ER, without perturbing LSG1-dependent recycling of NMD3 or modulation of LSG1 GTPase activity .

摘要

LSG1 是一种保守的 GTPase,参与核糖体组装。它对于核输出适配器 NMD3 从细胞质中的前 60S 亚基中逐出是必需的。在人类细胞中,LSG1 也已显示与主要存在于内质网上的囊泡相关膜蛋白相关蛋白 (VAP) 相互作用。VAP 与包含 FFAT 基序(酸性序列中的两个苯丙氨酸 (FF))的大量宿主蛋白相互作用,参与许多细胞功能,包括膜运输和脂质运输的调节。在这里,我们表明人 LSG1 通过非典型的 FFAT 样基序与 VAP 结合。该基序的缺失特异性地破坏了 LSG1 到 ER 的定位,而不会干扰 LSG1 依赖的 NMD3 再循环 或 LSG1 GTPase 活性的调节 。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f633/11376406/b070bbcfe573/TMCB_A_2384600_F0005_C.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f633/11376406/abe91c5a0992/TMCB_A_2384600_F0001_C.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f633/11376406/84daa03b0726/TMCB_A_2384600_F0002_C.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f633/11376406/c458cbbddc6c/TMCB_A_2384600_F0003_C.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f633/11376406/78b0d0e035d2/TMCB_A_2384600_F0004_C.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f633/11376406/b070bbcfe573/TMCB_A_2384600_F0005_C.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f633/11376406/abe91c5a0992/TMCB_A_2384600_F0001_C.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f633/11376406/84daa03b0726/TMCB_A_2384600_F0002_C.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f633/11376406/c458cbbddc6c/TMCB_A_2384600_F0003_C.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f633/11376406/78b0d0e035d2/TMCB_A_2384600_F0004_C.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/f633/11376406/b070bbcfe573/TMCB_A_2384600_F0005_C.jpg

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