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Blood, Vol. 96 No. 2 (July 15), 2000:
pp. 699-704
ZNF198-FGFR1 transforming activity depends on a novel
proline-rich ZNF198 oligomerization domain
Sheng Xiao,
Jennifer G. McCarthy,
Jon C. Aster, and
Jonathan A. Fletcher
From the Department of Pathology, Brigham and Women's Hospital, the
Dana-Farber Cancer Institute, and the Division of
Hematology-Oncology, Children's Hospital, Boston, MA.
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.
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