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Published online 24 July 2000. doi:10.1083/jcb.150.2.309
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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



Tim McGarveya, Emanuel Rosoninaa, Susan McCrackena, Qiyu Lia, Ramy Arnaoutb, Edwin Mientjesd, Jeffrey A. Nickersonc, Don Awreya, Jack Greenblatta, Gerard Grosveldd, and Benjamin J. Blencowea

a Banting and Best Department of Medical Research, C.H. Best Institute, University of Toronto, Toronto, Ontario, Canada M5G 1L6
b Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139
c Department of Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01655
d Department of Genetics, St. Jude Children's Research Hospital, Memphis, Tennessee 38105
Banting and Best Department of Medical Research, C.H. Best Institute, University of Toronto, 112 College Street, Room 410, Toronto, Ontario, Canada M5G 1L6.(416) 978-8528(416) 978-3016

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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