T-cell oncogene rhombotin-2 interacts with retinoblastoma-binding protein 2
被引:0
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作者:
Shifeng Mao
论文数: 0引用数: 0
h-index: 0
机构:St Jude Children's Research Hospital,Departments of Virology and Molecular Biology
Shifeng Mao
Geoffrey AM Neale
论文数: 0引用数: 0
h-index: 0
机构:St Jude Children's Research Hospital,Departments of Virology and Molecular Biology
Geoffrey AM Neale
Rakesh M Goorha
论文数: 0引用数: 0
h-index: 0
机构:St Jude Children's Research Hospital,Departments of Virology and Molecular Biology
Rakesh M Goorha
机构:
[1] St Jude Children's Research Hospital,Departments of Virology and Molecular Biology
[2] University of Tennessee,Department of Pathology
[3] Memphis Tennessee,undefined
来源:
Oncogene
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1997年
/
14卷
关键词:
oncogene;
rhombotin-2;
RBP2;
transcription;
D O I:
暂无
中图分类号:
学科分类号:
摘要:
The LIM domain protein rhombotin-2 (RBTN-2/TTG-2/Lmo2) has distinct functions in erythropoiesis and in T-cell leukemogenesis. Additional functions for RBTN2 are indicated by its expression in non-hematopoietic tissues. These diverse functions of RBTN2 are presumed to be accomplished through physical interaction with different protein partners that bind the LIM domains of RBTN2. To identify these proteins which may modulate the activity of RBTN2, a human cDNA library was screened using the yeast two-hybrid assay. Using the RBTN2 LIM domain region as `bait', the retinoblastoma-binding protein 2 (RBP2) was identified as a partner for RBTN2. The interaction between RBTN2 and RBP2 was confirmed using in vitro binding assays, and by co-immunoprecipitation of the two proteins. Deletion analysis showed the second LIM domain of RBTN2 was necessary and sufficient for binding to the last 69 amino acids of RBP2. The interaction between RBTN2 and RBP2 had a functional consequence: the combination of RBP2 and RBTN2 gave higher transcription in vitro, than RBTN2 alone. The interaction with RBP2 suggests two additional functions for RBTN2: (i) RBTN2 may directly affect the activity of RBP2, and/or (ii) RBTN2 may indirectly modulate the functions of the retinoblastoma protein by binding to RBP2.