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[Cancer Research 61, 3586-3590, May 1, 2001]
© 2001 American Association for Cancer Research

Advances in Brief

Oncogenic TLS/ERG and EWS/Fli-1 Fusion Proteins Inhibit RNA Splicing Mediated by YB-1 Protein1

Howard A. Chansky, Ming Hu, Dennis D. Hickstein and Liu Yang2

Department of Orthopedics, University of Washington School of Medicine, Seattle, Washington 98195 [H. A. C., M. H., L. Y.]; Medical Research Service, VA Puget Sound Health Care System, Seattle, Washington 98108 [H. A. C., M. H., L. Y.]; and Experimental Transplantation and Immunology, National Cancer Institute, Bethesda, Maryland 20892 [D. D. H.]

The translocation liposarcoma protein TLS has recently been shown to function as an adapter molecule coupling gene transcription to RNA splicing. Here we demonstrate that YB-1, a protein known to play important roles in transcription and translation, interacts with the COOH-terminal domains of TLS and the structurally related Ewing’s sarcoma protein EWS. Through this interaction, YB-1 is recruited to RNA polymerase II and promotes splicing of E1A pre-mRNA to the 13S isoform. This splicing function of YB-1 is inhibited by exogenous TLS/ERG or EWS/Fli-1 fusion proteins, which bind to RNA polymerase II but fail to recruit the YB-1 protein. In Ewing’s sarcoma cells that express endogenous EWS/Fli-1, this linkage between YB-1 and RNA Pol II via EWS (or TLS) was found to be defective. Together, these results suggest that TLS and EWS fusion proteins may contribute to malignant transformation through disruption of RNA splicing mediated by TLS- and EWS-binding proteins such as YB-1.




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Copyright © 2001 by the American Association for Cancer Research.