MATR3

Last update 08 May 2025

Basic Info

Synonyms

KIAA0723, MATR3, matrin 3

+ [4]

Introduction

May play a role in transcription or may interact with other nuclear matrix proteins to form the internal fibrogranular network. In association with the SFPQ-NONO heteromer may play a role in nuclear retention of defective RNAs. Plays a role in the regulation of DNA virus-mediated innate immune response by assembling into the HDP-RNP complex, a complex that serves as a platform for IRF3 phosphorylation and subsequent innate immune response activation through the cGAS-STING pathway (PubMed:28712728). Binds to N6-methyladenosine (m6A)-containing mRNAs and contributes to MYC stability by binding to m6A-containing MYC mRNAs (PubMed:32245947). May bind to specific miRNA hairpins (PubMed:28431233).

100 Clinical Results associated with MATR3

100 Translational Medicine associated with MATR3

0 Patents (Medical) associated with MATR3

232

Literatures (Medical) associated with MATR3

04 Mar 2025·Microbiology Spectrum

Development and characterization of a double-fluorescent HIV-1 reporter cellular model to tackle the Rev-dependent export pathway

Article

Author: Osiecka, Aleksandra ; Ali, Haider ; Dorman, Agnieszka ; Wadas, Jakub ; Pyrc, Krzysztof ; Kula-Pacurar, Anna

ABSTRACTThe Rev-dependent nuclear export of unspliced and singly-spliced transcripts of human immunodeficiency virus type 1 (HIV-1) constitutes a critical yet poorly characterized post-transcriptional event essential for effective viral replication. In this study, we engineered a dual-fluorescent HIV-1-based cellular reporter system to elucidate the mechanisms underpinning Rev-dependent export. By generating multiple stably integrated inducible cellular clones, we ensured the expression of two distinct fluorescent proteins, mKO2, and ECFP, from unspliced (Rev dependent) and multiply spliced (Rev independent) HIV-1 transcripts, respectively. Utilizing flow cytometry, we performed quantitative analyses of dual-fluorescent cell populations. The developed tool enables precise assessment of the Rev-dependent export, and we validated it using known inhibitors of this pathway (leptomycin D), as well as targeted depletion of MATR3, an essential cofactor of Rev, and CRNKL1, a repressor of unspliced HIV-1 RNA export.IMPORTANCEThe developed dual-fluorescent reporter system represents a powerful and handy tool for the identification and characterization of novel molecular players involved in the Rev-dependent export pathway. This system not only holds promise for advancing our understanding of human immunodeficiency virus type 1 (HIV-1) biology but also serves as an invaluable platform for high-throughput drug screening aimed at targeting post-transcriptional HIV-1 RNA processes, particularly nuclear export. Consequently, this study offers significant implications for the development of novel therapeutic strategies to eradicate the virus.

01 Mar 2025·Veterinary Microbiology

ASFV p30 interacts with CCAR2 and MATR3 to promote ASFV replication

Article

Author: Xiao, Yihong ; Wu, Bingrong ; Xu, Tiangang ; Zuo, Yuanyuan ; Wang, Zhiliang ; Yu, Jiarong ; Ge, Shengqiang ; Yin, Lei ; Li, Jinming ; Chu, Xuefei ; Qu, Hailong

African swine fever (ASF) is a highly contagious and lethal disease caused by the African swine fever virus (ASFV). Currently, effective vaccines are not available for the prevention and control of ASF. ASFV is susceptible to mutations as it has a large genome and encodes numerous proteins. In addition to evading the host immune response, ASFV utilizes host proteins to regulate its replication. The ASFV p30 protein is involved in virus internalization into the host cell and is expressed throughout the viral replication cycle, influencing viral replication. This study identified the host proteins that interact with p30 using mass spectrometry analysis. Immunoprecipitation analysis confirmed that the ASFV p30 protein interacted with the host proteins CCAR2 and MATR3, co-localizing with them in the cytoplasm. CCAR2 and MATR3 promoted ASFV replication. Conversely, ASFV infection upregulated the expression of CCAR2 and MATR3 in the host. Thus, the ASFV p30 protein regulates ASFV replication by interacting with CCAR2 and MATR3.

01 Mar 2025·Genes & Development

The Rbfox1/LASR complex controls alternative pre-mRNA splicing by recognition of multipart RNA regulatory modules

Article

Author: Lin, Chia-Ho ; Black, Douglas L ; Onwuzurike, Kelechi ; Peyda, Parham

The Rbfox proteins regulate alternative pre-mRNA splicing by binding to the RNA element GCAUG. In the nucleus, most of Rbfox is bound to the large assembly of splicing regulators (LASR), a complex of RNA-binding proteins that recognize additional RNA motifs. However, it remains unclear how the different subunits of the Rbfox/LASR complex act together to bind RNA and regulate splicing. We used a nuclease protection assay to map the transcriptome-wide footprints of Rbfox1/LASR on nascent cellular RNA. In addition to GCAUG, Rbfox1/LASR binds RNA motifs for LASR subunits hnRNPs M, H/F, and C and Matrin3. These elements are often arranged in tandem, forming multipart modules of RNA motifs. To distinguish contact sites of Rbfox1 from the LASR subunits, we analyzed a mutant Rbfox1(F125A) that has lost RNA binding but remains associated with LASR. Rbfox1(F125A)/LASR complexes no longer interact with GCAUG but retain binding to RNA elements for LASR. Splicing analyses reveal that in addition to activating exons through adjacent GCAUG elements, Rbfox can also stimulate exons near binding sites for LASR subunits. Minigene experiments demonstrate that these diverse elements produce a combined regulatory effect on a target exon. These findings illuminate how a complex of RNA-binding proteins can decode combinatorial splicing regulatory signals by recognizing groups of tandem RNA elements.

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