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ZNF198-FGFR1 transforming activity depends on a novel proline-rich ZNF198 oligomerization domain
S Xiao1, J G McCarthy, J C Aster
1Department of Pathology, Brigham and Women's Hospital, the Dana-Farber Cancer Institute, and the Division of Hematology-Oncology, Children's Hospital, Boston, MA.sxaio@rics.bwh.harvard.edu
Abstract:
An acquired chromosomal translocation, t(8;13)(p11;q11-12), observed in a distinctive type of stem cell leukemia/lymphoma syndrome, leads to the fusion of the 5' portion of ZNF198 and the 3' portion of FGFR1. ZNF198-FGFR1 fusion transcripts encode 4 to 10 zinc fingers, a proline-rich region, and the intracellular portion of the FGFR1 (fibroblast growth factor receptor 1) receptor tyrosine kinase. We demonstrate that the ZNF198 proline-rich region constitutes a novel self-association domain. When fused to the intracellular domain of FGFR1, the ZNF198 proline-rich region is sufficient to cause oligomerization, FGFR1 tyrosine kinase activation, and transformation of Ba/F3 cells to IL-3 independent growth. (Blood. 2000;96:699-704)