ArticleMolecular biology of the cell2002
A conserved Drosophila transportin-serine/arginine-rich (SR) protein permits nuclear import of Drosophila SR protein splicing factors and their antagonist repressor splicing factor 1.
Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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30 citing papers in PubMed, 54 citations in OpenAlex.
- The regulation of carnitine palmitoyltransferase 1 (Biochemistry and biophysics reports · 2024Article
- SR proteins in cancer: function, regulation, and small inhibitor.Cellular & molecular biology letters · 2024Review
- The RasGAP-associated endoribonuclease G3BP mediates stress granule assembly.The Journal of cell biology · 2023Article
- β-importin Tnpo-SR promotes germline stem cell maintenance and oocyte differentiation in female Drosophila.Developmental biology · 2023Article
- Inhibition of autophagy rescues muscle atrophy in a LGMDD2 Drosophila model.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- TNPO2 variants associate with human developmental delays, neurologic deficits, and dysmorphic features and alter TNPO2 activity in Drosophila.American journal of human genetics · 2021Article
- Transcribed sex-specific markers on the Y chromosome of the oriental fruit fly, Bactrocera dorsalis.BMC genetics · 2020Article
- Cytosolic calcium regulates cytoplasmic accumulation of TDP-43 through Calpain-A and Importin α3.eLife · 2020Article
- An Efficient Screen for Cell-Intrinsic Factors Identifies the Chaperonin CCT and Multiple Conserved Mechanisms as Mediating Dendrite Morphogenesis.Frontiers in cellular neuroscience · 2020Article
- tRNA dynamics between the nucleus, cytoplasm and mitochondrial surface: Location, location, location.Biochimica et biophysica acta. Gene regulatory mechanisms · 2018Review
- A Genetic Mosaic Screen Reveals Ecdysone-Responsive Genes Regulating Drosophila Oogenesis.G3 (Bethesda, Md.) · 2016Article
- Structural basis for nuclear import of splicing factors by human Transportin 3.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Article
- The HPV E2-Host Protein-Protein Interactions: A Complex Hijacking of the Cellular Network.The open virology journal · 2012Article
- Mutations affecting interaction of integrase with TNPO3 do not prevent HIV-1 cDNA nuclear import.Retrovirology · 2011Article
- The cargo-binding domain of transportin 3 is required for lentivirus nuclear import.Journal of virology · 2011Article
- Nuclear import by karyopherin-βs: recognition and inhibition.Biochimica et biophysica acta · 2011Review
- Re-localization of cellular protein SRp20 during poliovirus infection: bridging a viral IRES to the host cell translation apparatus.PLoS pathogens · 2011Article
- Transportin-SR is required for proper splicing of resistance genes and plant immunity.PLoS genetics · 2011Article
- Cyclic AMP-dependent protein kinase regulates the alternative splicing of tau exon 10: a mechanism involved in tau pathology of Alzheimer disease.The Journal of biological chemistry · 2011Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Members of the highly conserved serine/arginine-rich (SR) protein family are nuclear factors involved in splicing of metazoan mRNA precursors. In mammals, two nuclear import receptors, transportin (TRN)-SR1 and TRN-SR2, are responsible for targeting SR proteins to the nucleus. Distinctive features in the nuclear localization signal between Drosophila and mammalian SR proteins prompted us to examine the mechanism by which Drosophila SR proteins and their antagonist repressor splicing factor 1 (RSF1) are imported into nucleus. Herein, we report the identification and characterization of a Drosophila importin beta-family protein (dTRN-SR), homologous to TRN-SR2, that specifically interacts with both SR proteins and RSF1. dTRN-SR has a broad localization in the cytoplasm and the nucleus, whereas an N-terminal deletion mutant colocalizes with SR proteins in nuclear speckles. Far Western experiments established that the RS domain of SR proteins and the GRS domain of RSF1 are required for the direct interaction with dTRN-SR, an interaction that can be modulated by phosphorylation. Using the yeast model system in which nuclear import of Drosophila SR proteins and RSF1 is impaired, we demonstrate that complementation with dTRN-SR is sufficient to target these proteins to the nucleus. Together, the results imply that the mechanism by which SR proteins are imported to the nucleus is conserved between Drosophila and humans.
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