Reference Report

Reference
Citation	Allemand, E., Dokudovskaya, S., Bordonne, R., Tazi, J. (2002). 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. Mol. Biol. Cell 13(7): 2436--2447. (Export to RIS)
FlyBase ID	FBrf0151413
Publication Type	Research paper
PubMed ID	12134081
PubMed 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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Language of Publication	English
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Publication Type	Journal
Abbreviation	Mol. Biol. Cell
Title	Molecular Biology of the Cell
Publication Year	1992-
ISBN/ISSN	1059-1524
Data from Reference
Alleles (27)
	B52^{T:Avic\GFP-EGFP} B52^{ΔRRM.T:Avic\GFP-EGFP} B52^{ΔRS.T:Avic\GFP-EGFP} Hsap\SRSF1^{RS.T:Avic\GFP-EGFP} Hsap\SRSF1^{T:Avic\GFP-EGFP} Hsap\SRSF1^{ΔRS.T:Avic\GFP-EGFP} Hsap\SRSF2^{T:Avic\GFP-EGFP} Hsap\SRSF2^{ΔRRM.T:Avic\GFP-EGFP} Hsap\SRSF2^{ΔRS.T:Avic\GFP-EGFP} Rbp1^{T:Avic\GFP-EGFP} Rbp1^{ΔRRM.T:Avic\GFP-EGFP} Rbp1^{ΔRS.T:Avic\GFP-EGFP} Rsf1^{T:Avic\GFP-EGFP} Rsf1^{ΔGRS.T:Avic\GFP-EGFP} Rsf1^{ΔRRM.T:Avic\GFP-EGFP} SC35^{T:Avic\GFP-EGFP} SC35^{ΔRRM.T:Avic\GFP-EGFP} SC35^{ΔRS.T:Avic\GFP-EGFP} SF2^{RS.T:Avic\GFP-EGFP} SF2^{T:Avic\GFP-EGFP} SF2^{ΔRS.T:Avic\GFP-EGFP} T:Avic\GFP^EGFP Trn-SR^{T:Avic\GFP-EGFP} Trn-SR^{ΔN217.T:Avic\GFP-EGFP} x16^{T:Avic\GFP-EGFP} x16^{ΔRRM.T:Avic\GFP-EGFP} x16^{ΔRS.T:Avic\GFP-EGFP}
Genes (14)
	B52 Hsap\SRSF1 Hsap\SRSF2 Rbp1 Rsf1 SC35 SF2 snRNP-U1-70K sqd SRp30 T:Avic\GFP Trn Trn-SR x16