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Nucleic Acids Research 2005 33(9):2769-2780; doi:10.1093/nar/gki561
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Published online 13 May 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

Identification of CELF splicing activation and repression domains in vivo

Jin Han1 and Thomas A. Cooper1,2,*

1Department of Pathology, Baylor College of Medicine Houston, TX 77030, USA 2Department of Molecular and Cellular Biology, Baylor College of Medicine Houston, TX 77030, USA

*To whom correspondence should be addressed. Tel: +1 713 798 3141; Fax: +1 713 798 5838; Email: tcooper{at}bcm.tmc.edu

Received March 18, 2005. Revised April 20, 2005. Accepted April 20, 2005.

CUG-BP and ETR-3 like factor (CELF) proteins are regulators of pre-mRNA alternative splicing. We created a series of truncation mutants to identify the regions of CELF proteins that are required to activate and to repress alternative splicing of different exons. This analysis was performed in parallel on two CELF proteins, ETR-3 (CUG-BP2, NAPOR, BRUNOL3) and CELF4 (BRUNOL4). We identified a 20-residue region of CELF4 required for repression or activation, in contrast to ETR-3, for which the required residues are more disperse. For both ETR-3 and CELF4, distinct regions were required to activate splicing of two different alternative exons, while regions required for repression of an additional third exon overlapped with regions required for activation. Our results suggest that activation of different splicing events by individual CELF proteins requires separable regions, implying the nature of the protein–protein interactions required for activation are target-dependent. The finding that residues required for activation and repression overlap suggests either that the same region interacts with different proteins to mediate different effects or that interactions with the same proteins can have different effects on splicing due to yet-to-be defined downstream events. These results provide a foundation for identifying CELF-interacting proteins involved in activated and/or repressed splicing.


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