ZNF198-FGFR1 transforming activity depends on a novel proline-rich ZNF198 oligomerization domain.
ZNF198-FGFR1 transforming activity depends on a novel proline-rich ZNF198 oligomerization domain.
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DOI：
10.1182/blood.v96.2.699.014k53_699_704
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发表时间：
2000-07
期刊：
影响因子：
20.3
通讯作者：
S. Xiao;Jennifer McCarthy;J. Aster;J. Fletcher
中科院分区：
文献类型：
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作者：
S. Xiao;Jennifer McCarthy;J. Aster;J. Fletcher
在一种特殊类型的干细胞白血病/淋巴瘤综合征中观察到的获得性染色体易位t（8;13）（p11;q11-12）导致ZNF 198的5'部分与FGFR 1的3'部分融合。ZNF 198-FGFR 1融合转录本编码4 - 10个锌指、富含脯氨酸的区域和FGFR 1（成纤维细胞生长因子受体1）受体酪氨酸激酶的细胞内部分。我们证明了ZNF 198富含脯氨酸的区域构成了一个新的自缔合结构域。当与FGFR 1的胞内结构域融合时，ZNF 198富含脯氨酸的区域足以引起寡聚化、FGFR 1酪氨酸激酶激活和Ba/F3细胞转化为IL-3非依赖性生长。（血。2000;96：699-704）
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)