The TREX-2 protein complex is the key complex involved in the export of mRNA from the nucleus to the cytoplasm through the nuclear pores. Previously, a joint protein complex of TREX-2 with ORC was isolated in D. melanogaster. It was shown that the interaction of TREX-2 with ORC is necessary for efficient mRNA export from the nucleus to the cytoplasm. In this work, we showed that the TREX-2-ORC joint complex is also formed in human cells.
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| http://dx.doi.org/10.1134/S1607672923700552 | DOI Listing |
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[Drosophila melanogaster Paip2 Binds ENY2 and Interacts with the TREX-2 Complex in Histone mRNP Particles].
Mol Biol (Mosk)
December 2024
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, 119991 Russia.
ENY2 is an evolutionarily conserved multifunctional protein and is a member of several complexes that regulate various stages of gene expression. ENY2 is a subunit of the TREX-2 complex, which is necessary for the export of bulk mRNA from the nucleus to the cytoplasm through the nuclear pores in many eukaryotes. The wide range of ENY2 functions suggests that it can also associate with other protein factors or complexes.
View Article and Find Full Text PDFCellular NS1-BP protein interacts with the mRNA export receptor NXF1 to mediate nuclear export of influenza virus M mRNAs.
J Biol Chem
November 2024
Department of Cell Biology, University of Texas Southwestern Medical Center, Dallas, Texas, USA. Electronic address:
Article Synopsis
- Influenza A viruses contain eight genomic RNAs that are transcribed in the host cell nucleus, with two undergoing alternative splicing to produce M1 and M2 mRNAs.
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Xmas-2 Protein, the Core Protein of the TREX-2 mRNA Export Complex, Does not Determine the Specificity of ras2 mRNA Binding by the Complex.
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October 2024
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, 119991, Moscow, Russia.
The TREX-2 complex of eukaryotes is responsible for the export of a wide range of mRNAs from the nucleus to the cytoplasm. Previously, we showed that a subunit of the D. melanogaster TREX-2 complex, the PCID2 protein, has a domain that specifically interacts with RNA.
View Article and Find Full Text PDFPoint Mutations in the M Domain of PCID2 Impair Its Function in mRNA Export in Drosophila melanogaster.
Dokl Biol Sci
October 2024
Engelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
The PCID2 protein is a component of the eukaryotic TREX-2 complex, which is responsible for mRNA export from the nucleus into the cytoplasm. We have previously shown that Drosophila melanogaster PCID2 is involved in specific mRNA recognition and identified the key amino acids responsible for its interaction with the ras2 RNA. In this work, point mutations of the amino acids were shown to disrupt the PCID2 interaction with cell RNAs and to distort the export of polyA-containing mRNAs from the nucleus into the cytoplasm in Drosophila cells.
View Article and Find Full Text PDFCarcinogenesis caused by transcription-coupled DNA damage through GANP and other components of the TREX-2 complex.
Pathol Int
March 2024
Department of Diagnostic Pathology, Kindai University Hospital, Osaka, Japan.
Perturbation of genes is important for somatic hypermutation to increase antibody affinity during B-cell immunity; however, it may also promote carcinogenesis. Previous studies have revealed that transcription is an important process that can induce DNA damage and genomic instability. Transciption-export-2 (TREX-2) complex, which regulates messenger RNA (mRNA) nuclear export, has been studied in the budding yeast Saccharomyces cerevisiae; however, recent studies have started investigating the molecular function of the mammalian TREX-2 complex.
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