The Acute Myeloid Leukemia-Associated Protein, Dek, Forms a Splicing-Dependent Interaction with Exon-Product Complexes

Author:

McGarvey Tim1,Rosonina Emanuel1,McCracken Susan1,Li Qiyu1,Arnaout Ramy2,Mientjes Edwin3,Nickerson Jeffrey A.4,Awrey Don1,Greenblatt Jack1,Grosveld Gerard3,Blencowe Benjamin J.1

Affiliation:

1. Banting and Best Department of Medical Research, C.H. Best Institute, University of Toronto, Toronto, Ontario, Canada M5G 1L6

2. Center for Cancer Research, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139

3. Department of Genetics, St. Jude Children's Research Hospital, Memphis, Tennessee 38105

4. Department of Cell Biology, University of Massachusetts Medical School, Worcester, Massachusetts 01655

Abstract

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.

Publisher

Rockefeller University Press

Subject

Cell Biology

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