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© The Rockefeller University Press,
0021-9525/2000//309 $5.00
The Journal of Cell Biology, Volume 150, Number 2,
, 2000 309-320
Original Article |
The Acute Myeloid Leukemia-Associated Protein, Dek, Forms a Splicing-Dependent Interaction with Exon-Product Complexes
b.blencowe{at}utoronto.ca
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.
Key Words: SR proteins spliceosome mRNP mRNA transport
© 2000 The Rockefeller University Press
Abbreviations used in this paper: AML, acute myeloid leukemia; CTD, COOH-terminal domain; ESE, exonic splicing enhancer; EV, epidermodysplasia verruciformis; hnRNP, heteronucleoriboprotein; HPV, human papillomavirus; pets, peri-ets; rAb, rabbit polyclonal antibody; RNA pol II, RNA polymerase II; RS domain, domain rich in alternating arginine and serine residues; snRNPs, small nuclear ribonucleoprotein particles; SR protein, serine/arginine-repeat protein.
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