The acute myeloid leukemia-associated protein, DEK, forms a splicing-dependent interaction with exon-product complexes.

The acute myeloid leukemia-associated protein, DEK, forms a splicing-dependent interaction with exon-product complexes.
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DOI:
10.1083/jcb.150.2.309
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发表时间:
2000-07-24
期刊:
The Journal of cell biology
影响因子:
--
通讯作者:
Blencowe BJ
Blencowe BJ
中科院分区:
其他
文献类型:
--
作者:
McGarvey T;Rosonina E;McCracken S;Li Q;Arnaout R;Mientjes E;Nickerson JA;Awrey D;Greenblatt J;Grosveld G;Blencowe BJ

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DEK is an ∼45-kD phosphoprotein that is fused to the nucleoporin CAN as a result of a (6;9) chromosomal translocation in a subset of acute myeloid leukemias (AMLs). It has also been identified as an autoimmune antigen in juvenile rheumatoid arthritis and other rheumatic diseases. Despite the association of DEK with several human diseases, its function is not known. In this study, we demonstrate that DEK, together with SR proteins, associates with the SRm160 splicing coactivator in vitro. DEK is recruited to splicing factor-containing nuclear speckles upon concentration of SRm160 in these structures, indicating that DEK and SRm160 associate in vivo. We further demonstrate that DEK associates with splicing complexes through interactions mediated by SR proteins. Significantly, DEK remains bound to the exon-product RNA after splicing, and this association requires the prior formation of a spliceosome. Thus, DEK is a candidate factor for controlling postsplicing steps in gene expression that are influenced by the prior removal of an intron from pre-mRNA.
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发表时间: 1994-11
期刊: The Journal of cell biology
影响因子: --
作者:
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通讯作者: Sharp PA
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