ArticleThe EMBO journal2007
SAGA and a novel Drosophila export complex anchor efficient transcription and mRNA export to NPC.
Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.
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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.
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Who cites it
104 citing papers in PubMed, 181 citations in OpenAlex.
- The Proteins of the TREX-2 mRNA Export Complex Are Involved in Anchoring of the Sgf11 Protein Localized in Proximity to the Nuclear Pore in Drosophila melanogaster.Doklady. Biochemistry and biophysics · 2026Article
- ENY2 Protein Is Present at the Histone Locus Body HLB As Part of Complexes with Different Functions in Transcription and mRNA Export.Doklady. Biochemistry and biophysics · 2026Article
- Article
- SAGA Transcription Coactivator Complex Is Associated with Histone Locus Body HLB.Doklady. Biochemistry and biophysics · 2025Article
- Peculiarities of theInternational journal of molecular sciences · 2025Article
- TREX-2 mRNA Export Complex Interacts with HLB Component FLASH and Is Recruited to Processed Histone mRNAs.Doklady. Biochemistry and biophysics · 2025Article
- The nuclear pore complex acts as a hub for pri-miRNA transcription and processing in plants.Nucleic acids research · 2025Article
- Nup153 and TPR/Megator Interact with TREX-2 Subunits and Are Essential for TREX-2-Dependent Nuclear Export ofInternational journal of molecular sciences · 2025Article
- Interdomain Interactions of the PCID2 Protein, One of the Subunits of the TREX-2 mRNA Export Complex in Drosophila melanogaster.Doklady. Biochemistry and biophysics · 2025Article
- Point Mutations in the M Domain of PCID2 Impair Its Function in mRNA Export in Drosophila melanogaster.Doklady biological sciences : proceedings of the Academy of Sciences of the USSR, Biological sciences sections · 2024Article
- 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.Doklady. Biochemistry and biophysics · 2024Article
- Nuclear mRNA export.Acta biochimica et biophysica Sinica · 2024Review
- TREX-2-ORC Complex of D. melanogaster Participates in Nuclear Export of Histone mRNA.Doklady. Biochemistry and biophysics · 2024Article
- The Human TREX-2 Complex Interacts with Subunits of the ORC Complex.Doklady. Biochemistry and biophysics · 2023Article
- Interaction of mRNA with the C-Terminal Domain of PCID2, a Subunit of the TREX-2 Complex, Is Required for Its Export from the Nucleus to the Cytoplasm in Drosophila melanogaster.Doklady. Biochemistry and biophysics · 2023Article
- PCID2 Subunit of theCurrent issues in molecular biology · 2023Article
- The Xmas-2 Protein of Drosophila melanogaster Undergoes Cleavage into Two Fragments.Doklady. Biochemistry and biophysics · 2023Article
- Nuclear pore complex acetylation regulates mRNA export and cell cycle commitment in budding yeast.The EMBO journal · 2022Article
- Sus1 maintains a normal lifespan through regulation of TREX-2 complex-mediated mRNA export.Aging · 2022Article
- Nuclear mRNA Export and Aging.International journal of molecular sciences · 2022Review
44 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SAGA/TFTC-type multiprotein complexes play important roles in the regulation of transcription. We have investigated the importance of the nuclear positioning of a gene, its transcription and the consequent export of the nascent mRNA. We show that E(y)2 is a subunit of the SAGA/TFTC-type histone acetyl transferase complex in Drosophila and that E(y)2 concentrates at the nuclear periphery. We demonstrate an interaction between E(y)2 and the nuclear pore complex (NPC) and show that SAGA/TFTC also contacts the NPC at the nuclear periphery. E(y)2 forms also a complex with X-linked male sterile 2 (Xmas-2) to regulate mRNA transport both in normal conditions and after heat shock. Importantly, E(y)2 and Xmas-2 knockdown decreases the contact between the heat-shock protein 70 (hsp70) gene loci and the nuclear envelope before and after activation and interferes with transcription. Thus, E(y)2 and Xmas-2 together with SAGA/TFTC function in the anchoring of a subset of transcription sites to the NPCs to achieve efficient transcription and mRNA export.
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Registered trials
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.