Abstract
YT521-B is a ubiquitously expressed nuclear protein that changes alternative splice site usage in a concentration dependent manner. YT521-B is located in a dynamic nuclear compartment, the YT body. We show that YT521-B is tyrosine phosphorylated by c-Abl in the nucleus. The protein shuttles between nucleus and cytosol, where it can be phosphorylated by c-Src or p59fyn. Tyrosine phosphorylation causes dispersion of YT521-B from YT bodies to the nucleoplasm. Whereas YT bodies are soluble in non-denaturing buffers, the phosphorylated, dispersed form is non-soluble. Non-phosphorylated YT521-B changes alternative splice site selection of the IL-4 receptor, CD44 and SRp20, but phosphorylation of c-Abl minimizes this concentration dependent effect. We propose that tyrosine phosphorylation causes sequestration of YT521-B in an insoluble nuclear form, which abolishes the ability of YT521-B to change alternative splice sites.
Original language | English |
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Pages (from-to) | 1535-1549 |
Number of pages | 15 |
Journal | Human Molecular Genetics |
Volume | 13 |
Issue number | 15 |
DOIs | |
State | Published - Aug 1 2004 |
Bibliographical note
Funding Information:We thank Nora Heisterkamp, Pamela Schwartzberg, G. Superti-Furga, A.L. Tyner and J. Zhang for providing expression clones and Andre Gessner for providing c-DNAs. This work was supported by the Deutsche Forschungsgemeinschaft.
Funding
We thank Nora Heisterkamp, Pamela Schwartzberg, G. Superti-Furga, A.L. Tyner and J. Zhang for providing expression clones and Andre Gessner for providing c-DNAs. This work was supported by the Deutsche Forschungsgemeinschaft.
Funders | Funder number |
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Deutsche Forschungsgemeinschaft |
ASJC Scopus subject areas
- Molecular Biology
- Genetics
- Genetics(clinical)