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Updated: Jul 11, 2026
08:38
Phospho Flow Cytometry with Fluorescent Cell Barcoding for Single Cell Signaling Analysis and Biomarker Discovery
Published on: October 4, 2018
DX16 is a novel SR protein phosphorylated by DOA
Yongqi Wan1, Mingkuan Sun, Shanzhi Wang
1Department of Genetics and Developmental Biology, Southeast University Medical School, The Key Laboratory of Developmental Genes and Human Disease, Ministry of Education, Nanjing, PR China.
Molecular and Cellular Biochemistry
|September 11, 2007
Summary
Drosophila
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- Serine-arginine-rich (SR) proteins are crucial for pre-mRNA splicing and alternative splicing regulation.
- DX16 is a member of the SR protein family in Drosophila, a fruit fly model organism.
Purpose of the Study:
- To investigate the function of DX16 by identifying its interacting proteins.
- To understand the molecular mechanisms underlying DX16's role in splicing.
Main Methods:
- Yeast two-hybrid assays to screen for interacting proteins.
- GST-pull down assays to confirm interactions.
- In vitro phosphorylation assays and in vivo phosphorylation analysis.
- Immunofluorescence microscopy to determine protein expression patterns.
Main Results:
- DX16 interacts with CG7564 (a U1 snRNP subunit), RBP1 (an SR protein), and DOA (an SR protein kinase).
- Specific regions of DOA (serine- and arginine-rich regions) are necessary for binding DX16.
- DX16 is phosphorylated by DOA in vitro and is highly phosphorylated in vivo.
- Both DOA and DX16 show high expression in the embryonic central nervous system of Drosophila.
Conclusions:
- DX16 is a novel SR protein that is phosphorylated by DOA.
- DX16 likely participates in spliceosome complex formation through its interactions with other splicing factors.
- The interaction and phosphorylation of DX16 by DOA suggest a regulatory role in Drosophila splicing, particularly in the nervous system.
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