Evidence map›Paper›PMID 41083635›Full record

ArticleDoklady. Biochemistry and biophysics2025

TREX-2 mRNA Export Complex Interacts with HLB Component FLASH and Is Recruited to Processed Histone mRNAs.

M M Kurshakova, Y A Yakusheva, S G Georgieva

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Article in Doklady. Biochemistry and biophysics, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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1 · What the graph read from it

What it found

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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

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Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

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PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors.

M M KurshakovaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia. kursha@mail.ru.
Y A YakushevaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.
S G GeorgievaEngelhardt Institute of Molecular Biology, Russian Academy of Sciences, Moscow, Russia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Disruption of the normal expression of histone genes lead to the development of various pathologies. One of the key stages of gene expression is the export of mRNA from the nucleus to the cytoplasm. The TREX-2 protein complex regulates the export of the majority of poly(A)-containing mRNAs. Previously, we demonstrated that TREX-2 is also associated with histone mRNP particles and participates in the nuclear export of histone mRNAs, which lack poly(A)-tails. In this study we investigated the interaction of TREX-2 proteins with the histone mRNA processing machinery. It was shown that TREX-2 interacts with the FLASH protein, a key protein of the specialized histone mRNA processing machinery and a component of the histone locus body (HLB). The TREX-2 complex is recruited through its interaction with FLASH to processed histone mRNAs.

Indexed as

ExodeoxyribonucleasesHistonesNuclear ProteinsPhosphoproteinsRNA, MessengerActive Transport, Cell NucleusCell NucleusHeLa CellsHumansRibonucleoproteinsExodeoxyribonucleasesHistonesNuclear ProteinsPhosphoproteinsRibonucleoproteinsRNA, MessengerTREX2 protein, humanENY2FLASHhistone genesHLBmRNA exportORCPCID2TREX-2Xmas-2

Identifiers

PMID41083635

What OpenQuestion holds

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Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.