DX16 is a novel SR protein phosphorylated by DOA |
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Authors: | Yongqi Wan Mingkuan Sun Shanzhi Wang Li Liu Liudi Yuan Wei Xie |
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Institution: | (1) Department of Genetics and Developmental Biology, Southeast University Medical School, The Key Laboratory of Developmental Genes and Human Disease, Ministry of Education, 87 Dingjiaqiao Road, Nanjing, 210009, P.R. China |
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Abstract: | The serine-arginine-rich (SR) proteins belong to a conserved splicing factor family that not only is essential for constitutive
pre-mRNA splicing, but also plays important roles in regulation of alternative splicing. Dx16 is a member of SR protein family in Drosophila. In order to get more insight of dx16 function, we identified the proteins interacting with DX16 through yeast two-hybrid and GST-pull down assays. DX16 interacts
with the U1 snRNP subunit CG7564, the SR protein RBP1 and the SR protein kinase DOA. The first and second serine-and arginine-rich
regions of DOA are required for the interaction between DOA and DX16. DX16 could be phosphorylated by DOA in vitro and DX16 is highly phosphorylated in vivo. Immunofluorescence microscopy results reveal that doa and dx16 are both highly expressed in embryonic central nervous system. These results suggest that DX16 could be a novel SR protein
phosphorylated by DOA and it may participate in the formation of splicing complex through its interactions with other splicing
related proteins. |
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Keywords: | DX16 SR protein Phosphorylation |
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