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Human Molecular Genetics Advance Access originally published online on June 2, 2004
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Human Molecular Genetics, 2004, Vol. 13, No. 15 1535-1549
DOI: 10.1093/hmg/ddh167
Human Molecular Genetics, Vol. 13, No. 15 © Oxford University Press 2004; all rights reserved

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

Ilona Rafalska1,{dagger}, Zhaiyi Zhang1,{dagger}, Natalya Benderska1, Horst Wolff3, Annette M. Hartmann2, Ruth Brack-Werner3 and Stefan Stamm1,*

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

Received February 2, 2004; Revised April 1, 2004; Accepted May 18, 2004

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.

* To whom correspondence should be addressed. Tel: +49 91318524622; Fax: +49 91318524605; Email: stefan{at}stamms-lab.net


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