IVNS1ABP

Last update 23 Jan 2025

Basic Info

Synonyms

ARA3, Aryl hydrocarbon receptor-associated protein 3, FLARA3

+ [13]

Introduction

Involved in many cell functions, including pre-mRNA splicing, the aryl hydrocarbon receptor (AHR) pathway, F-actin organization and protein ubiquitination. Plays a role in the dynamic organization of the actin skeleton as a stabilizer of actin filaments by association with F-actin through Kelch repeats (By similarity). Protects cells from cell death induced by actin destabilization (By similarity). Functions as modifier of the AHR/Aryl hydrocarbon receptor pathway increasing the concentration of AHR available to activate transcription (PubMed:16582008). In addition, functions as a negative regulator of BCR(KLHL20) E3 ubiquitin ligase complex to prevent ubiquitin-mediated proteolysis of PML and DAPK1, two tumor suppressors (PubMed:25619834). Inhibits pre-mRNA splicing (in vitro) (PubMed:9696811). (Microbial infection) Involved in the alternative splicing of influenza A virus M1 mRNA through interaction with HNRNPK, thereby facilitating the generation of viral M2 protein.

100 Clinical Results associated with IVNS1ABP

100 Translational Medicine associated with IVNS1ABP

0 Patents (Medical) associated with IVNS1ABP

128

Literatures (Medical) associated with IVNS1ABP

01 Mar 2025·Veterinary Microbiology

Mink enteritis virus infection induced cell cycle arrest and autophagy for its replication

Article

Author: Zhi-Juan, Li ; Lu-Jiao, Dong ; Zhi-Jing, Xie ; Wen-Qian, Li ; Hua, Fan ; Jun, Peng ; Hui-Ning, Zhang ; Ying-Li, Sun

Mink enteritis virus (MEV) is an important pathogen causing mink viral enteritis. The mechanisms of cell cycle arrest induced by MEV infection and the roles of autophagy in MEV replication remain unclear. In this study, the roles of MEV NS1 protein in inducing cell cycle arrest were investigated, using the in vitro CRFK cell models. As a result, MEV infection increased the proportion of the cells in S phase, inducing S phase arrest. MEV NS1 protein also led to cycle arrest in S phase. And the deletions of NLS and TAD significantly weakened the ability of NS1 protein to cause cycle arrest in S phase, and NLS and TAD were the indispensable domains of NS1 protein. Furthermore, proteome profiling of the cells infected with MEV at the early stage demonstrated that the autophagy-related protein TRIM23 was significantly up-regulated during MEV infection. To investigate the effects of TRIM23 on MEV replication, the cell models were established, using siRNAs targeting TRIM23. The knockdown of TRIM23 resulted in the decreases in the levels of TBK1 protein and the phosphorylated p62 protein, and an increase in the level of p62 protein in the cells infected with MEV, indirectly influencing virus replication. The findings implied that S phase arrest and the up-regulated TRIM23 induced by MEV infection played the important roles in MEV replication.

01 Feb 2025·Virology

RTP4 restricts influenza A virus infection by targeting the viral NS1 protein

Article

Author: Zheng, Tian ; Wang, Jianwei ; Zhao, Shiyi ; Zhuo, Zhou ; Lv, Xueying ; Lei, Xiaobo ; Ren, Lili ; Wang, Jingfeng

The influenza A virus evades the host innate immune response to establish infection by inhibiting RIG-I activation through its nonstructural protein 1 (NS1). Here, we reported that receptor-transporting protein 4 (RTP4), an interferon-stimulated gene (ISG), targets NS1 to inhibit influenza A virus infection. Depletion of RTP4 significantly increased influenza A virus multiplication, while NS1-deficient viruses were unaffected. Mechanistically, RTP4 interacts with NS1 in an RNA-dependent manner and sequesters it from the TRIM25-RIG-I complex, thereby restoring TRIM25-mediated RIG-I K63-linked ubiquitination and subsequent activation of IRF3. Antiviral activity of RTP4 requires the evolutionarily conserved CXXC motifs and an H149 residue in the zinc finger domain, mutations of which disrupted RTP4-NS1 interaction and abrogated the ability of RTP4 to rescue RIG-I-mediated signaling. Collectively, our findings provided insights into the mechanism by which an ISG restricts influenza A virus replication by reactivating host antiviral signaling.

01 Nov 2024·Journal of Biological Chemistry

Cellular NS1-BP protein interacts with the mRNA export receptor NXF1 to mediate nuclear export of influenza virus M mRNAs

Article

Author: Fontoura, Beatriz M A ; Cagatay, Tolga ; He, Zhiyu ; Vazhavilla, Ashley ; Aslam, Sadaf ; Angelos, Alexia E ; Aksenova, Vasilisa ; García-Sastre, Adolfo ; Esparza, Matthew ; Dasso, Mary ; Ren, Yi ; Zhang, Ke ; Xie, Dongqi ; Cornelius, Serena

Influenza A viruses have eight genomic RNAs that are transcribed in the host cell nucleus. Two of the viral mRNAs undergo alternative splicing. The M1 mRNA encodes the matrix protein 1 (M1) and is also spliced into M2 mRNA, which encodes the proton channel matrix protein 2 (M2). Our previous studies have shown that the cellular Non-Structural protein 1 (NS1)-binding protein (NS1-BP) interacts with the viral NS1 and M1 mRNA to promote M1 to M2 splicing. Another pool of NS1 protein binds the mRNA export receptor nuclear RNA export factor-1 (NXF1), leading to nuclear retention of cellular mRNAs. Here, we show a series of biochemical and cell biological findings that suggest a model for nuclear export of M1 and M2 mRNAs despite the mRNA nuclear export inhibition imposed by the viral NS1 protein. NS1-BP competes with NS1 for NXF1 binding, allowing the recruitment of NXF1 to the M mRNAs after splicing. NXF1 then binds germinal center-associated nuclear protein, a member of the transcription and export complex-2. Although both NS1 and NS1-BP remain in complex with germinal center-associated nuclear protein-NXF1, they dissociate once this complex docks at the nuclear pore complex, and the M mRNAs are translocated to the cytoplasm. Since this mRNA nuclear export pathway is key for expression of M1 and M2 proteins that function in viral intracellular trafficking and budding, these viral-host interactions are critical for influenza virus replication.

Analysis

Perform a panoramic analysis of this field.

view full example data

Chat with Hiro

Get started for free today!

Accelerate Strategic R&D decision making with Synapse, PatSnap’s AI-powered Connected Innovation Intelligence Platform Built for Life Sciences Professionals.

Start your data trial now!

Synapse data is also accessible to external entities via APIs or data packages. Empower better decisions with the latest in pharmaceutical intelligence.

Bio

Bio Sequences Search & Analysis

Chemical

Chemical Structures Search & Analysis

IVNS1ABP

Basic Info

Related

Analysis