Abstract:
:In many human cancers, tumor-specific chromosomal rearrangements are known to create chimeric products with the ability to transform cells. The EWS/WT1 protein is such a fusion product, resulting from a t(11;22) chromosomal translocation in desmoplastic small round cell tumors, where 265 aa from the EWS amino terminus are fused to the DNA binding domain of the WT1 tumor suppressor gene. Herein, we find that EWS/WT1 is phosphorylated in vivo on serine and tyrosine residues and that this affects DNA binding and homodimerization. We also show that EWS/WT1 can interact with, and is a substrate for, modification on tyrosine residues by c-Abl. Tyrosine phosphorylation of EWS/WT1 by c-Abl negatively regulates its DNA binding properties. These results indicate that the biological activity of EWS/WT1 is closely linked to its phosphorylation status.
journal_name
Proc Natl Acad Sci U S Aauthors
Kim J,Lee JM,Branton PE,Pelletier Jdoi
10.1073/pnas.96.25.14300keywords:
subject
Has Abstractpub_date
1999-12-07 00:00:00pages
14300-5issue
25eissn
0027-8424issn
1091-6490journal_volume
96pub_type
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