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

Rafalska, Ilona, Zhang, Zhaiyi, Benderska, Natalya, Wolff, Horst, Hartmann, Annette M., Brack-Werner, Ruth, Stamm, Stefan·2004·Human Molecular Genetics
DOI 10.1093/hmg/ddh167
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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 p59(fyn). 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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Metadata

Authors
Rafalska, I., Zhang, Z., Benderska, N., Wolff, H., Hartmann, A. M., Brack-Werner, R., & Stamm, S.
Venue
Human Molecular Genetics
Publisher
Oxford University Press (OUP)
Published
2004-06-02
Volume
13
Issue
15
Pages
1535-1549
ISSN
  • 1460-2083
  • 0964-6906
DOI
10.1093/hmg/ddh167
Cited by
54
References
2
Language
en

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