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RanBP2/Nup358 介导 STAT1 的 SUMO 化并拮抗干扰素-α介导的抗病毒先天免疫。

RanBP2/Nup358 Mediates Sumoylation of STAT1 and Antagonizes Interferon-α-Mediated Antiviral Innate Immunity.

机构信息

Department of Immunology, School of Basic Medical Sciences, Fujian Medical University, Fuzhou 350108, China.

Department of Biochemistry, University of Toronto, Toronto, ON M5G 1M1, Canada.

出版信息

Int J Mol Sci. 2023 Dec 25;25(1):299. doi: 10.3390/ijms25010299.

DOI:10.3390/ijms25010299
PMID:38203469
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC10778711/
Abstract

Type I interferon (IFN-I)-induced signaling plays a critical role in host antiviral innate immune responses. Despite this, the mechanisms that regulate this signaling pathway have yet to be fully elucidated. The nucleoporin Ran Binding Protein 2 (RanBP2) (also known as Nucleoporin 358 KDa, Nup358) has been implicated in a number of cellular processes, including host innate immune signaling pathways, and is known to influence viral infection. In this study, we documented that RanBP2 mediates the sumoylation of signal transducers and activators of transcription 1 (STAT1) and inhibits IFN-α-induced signaling. Specifically, we found that RanBP2-mediated sumoylation inhibits the interaction of STAT1 and Janus kinase 1 (JAK1), as well as the phosphorylation and nuclear accumulation of STAT1 after IFN-α stimulation, thereby antagonizing the IFN-α-mediated antiviral innate immune signaling pathway and promoting viral infection. Our findings not only provide insights into a novel function of RanBP2 in antiviral innate immunity but may also contribute to the development of new antiviral therapeutic strategies.

摘要

I 型干扰素（IFN-I）诱导的信号转导在宿主抗病毒固有免疫反应中发挥着关键作用。尽管如此，调节这种信号通路的机制尚未完全阐明。核孔蛋白 Ran 结合蛋白 2（RanBP2）（也称为核孔蛋白 358 kDa，Nup358）已被牵涉到许多细胞过程中，包括宿主固有免疫信号通路，并已知会影响病毒感染。在这项研究中，我们记录到 RanBP2 介导信号转导和转录激活因子 1（STAT1）的 sumoylation，并抑制 IFN-α诱导的信号转导。具体而言，我们发现 RanBP2 介导的 sumoylation 抑制了 STAT1 和 Janus 激酶 1（JAK1）之间的相互作用，以及 IFN-α刺激后 STAT1 的磷酸化和核积累，从而拮抗 IFN-α介导的抗病毒固有免疫信号通路并促进病毒感染。我们的发现不仅为 RanBP2 在抗病毒固有免疫中的新功能提供了深入了解，而且可能为新的抗病毒治疗策略的发展做出贡献。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/040a/10778711/7b3681fbceba/ijms-25-00299-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/040a/10778711/e6ea381cc235/ijms-25-00299-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/040a/10778711/127217d1bfe7/ijms-25-00299-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/040a/10778711/3ecba9b4f61c/ijms-25-00299-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/040a/10778711/1bebcf6786ef/ijms-25-00299-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/040a/10778711/f639e0120909/ijms-25-00299-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/040a/10778711/7b3681fbceba/ijms-25-00299-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/040a/10778711/e6ea381cc235/ijms-25-00299-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/040a/10778711/127217d1bfe7/ijms-25-00299-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/040a/10778711/3ecba9b4f61c/ijms-25-00299-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/040a/10778711/1bebcf6786ef/ijms-25-00299-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/040a/10778711/f639e0120909/ijms-25-00299-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/040a/10778711/7b3681fbceba/ijms-25-00299-g006.jpg

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本文引用的文献

[1]
Omicron SARS-CoV-2 Neutralization from Inactivated and ZF2001 Vaccines.

N Engl J Med. 2022-7-21

[2]
Architecture of the cytoplasmic face of the nuclear pore.

Science. 2022-6-10

[3]
Roles of Nucleoporin RanBP2/Nup358 in Acute Necrotizing Encephalopathy Type 1 (ANE1) and Viral Infection.

Int J Mol Sci. 2022-3-24

[4]
SARS-CoV-2 NSP13 helicase suppresses interferon signaling by perturbing JAK1 phosphorylation of STAT1.

Cell Biosci. 2022-3-22

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SUMOylation in Viral Replication and Antiviral Defense.

Adv Sci (Weinh). 2022-3

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Viruses, SUMO, and immunity: the interplay between viruses and the host SUMOylation system.

J Neurovirol. 2021-8

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T-cell receptor (TCR) signaling promotes the assembly of RanBP2/RanGAP1-SUMO1/Ubc9 nuclear pore subcomplex via PKC-θ-mediated phosphorylation of RanGAP1.

Elife. 2021-6-10

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Crosstalk between nucleocytoplasmic trafficking and the innate immune response to viral infection.

J Biol Chem. 2021-7

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The miRISC component AGO2 has multiple binding sites for Nup358 SUMO-interacting motif.

Biochem Biophys Res Commun. 2021-6-4

[10]
RanBP2/Nup358 enhances miRNA activity by sumoylating Argonautes.

PLoS Genet. 2021-2

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