NDLI: The PTB interacting protein raver1 regulates α-tropomyosin alternative splicing

Content Provider	PubMed Central
Author	Natalia, Gromak Rideau, Alexis Southby, Justine Scadden, A. D. J. Gooding, Clare Stefan, Hüttelmaier Singer, Robert H. Smith, Christopher W. J.
Copyright Year	2003
Abstract	Regulated switching of the mutually exclusive exons 2 and 3 of α-tropomyosin (TM) involves repression of exon 3 in smooth muscle cells. Polypyrimidine tract-binding protein (PTB) is necessary but not sufficient for regulation of TM splicing. Raver1 was identified in two-hybrid screens by its interactions with the cytoskeletal proteins actinin and vinculin, and was also found to interact with PTB. Consistent with these interactions raver1 can be localized in either the nucleus or cytoplasm. Here we show that raver1 is able to promote the smooth muscle-specific alternative splicing of TM by enhancing PTB-mediated repression of exon 3. This activity of raver1 is dependent upon characterized PTB-binding regulatory elements and upon a region of raver1 necessary for interaction with PTB. Heterologous recruitment of raver1, or just its C-terminus, induced very high levels of exon 3 skipping, bypassing the usual need for PTB binding sites downstream of exon 3. This suggests a novel mechanism for PTB-mediated splicing repression involving recruitment of raver1 as a potent splicing co-repressor.
Related Links	http://dx.doi.org/10.1093/emboj/cdg609
Ending Page	6364
Page Count	9
Starting Page	6356
File Format	PDF
ISSN	14602075
e-ISSN	14602075
Journal	The EMBO Journal
Issue Number	23
Volume Number	22
Language	English
Publisher	Oxford University Press
Publisher Date	2003-12-01
Access Restriction	Open
Rights Holder	Oxford University Press
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Immunology and Microbiology(all) Neuroscience(all) Molecular Biology Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Neuroscience Immunology and Microbiology Medicine Molecular Biology

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