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Human Molecular Genetics Advance Access published online on June 2, 2004
Human Molecular Genetics, doi:10.1093/hmg/ddh167
© 2004 by Oxford University Press
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Article

The intranuclear localization and function of YT521-B is regulated by tyrosine phosphorylation

Ilona Rafalska 1, Zhaiyi Zhang 1, Natalya Benderska 1, Horst Wolff 2, Annette M. Hartmann 3, Ruth Brack-Werner 2, Stefan Stamm 1*

1 University of Erlangen, Institute for Biochemistry, Fahrstraße 17, 91054 Erlangen
2 Institute fuer Molecular Virology, GSF-Forschungszentrum fuer Umwelt und Gesundheit, Ingolstaedter Landstr. 1, D-85764 Neuherberg
3 Molecular Neurobiology, Department of Psychiatry, Ludwig-Maximilian-University, Nussbaumstr. 7, D-80336 Munich

* To whom correspondence should be addressed. E-mail: stefan{at}stamms-lab.net.


  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.


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