Phosphorylation switches the general splicing repressor SRp38 to a sequence-specific activator
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چکیده
منابع مشابه
Multiple properties of the splicing repressor SRp38 distinguish it from typical SR proteins.
The SR protein SRp38 is a general splicing repressor that is activated by dephosphorylation during mitosis and in response to heat shock. Here we describe experiments that provide insights into the mechanism by which SRp38 functions in splicing repression. We first show that SRp38 redistributes and colocalizes with snRNPs, but not with a typical SR protein, SC35, during mitosis and following he...
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SR proteins constitute a family of pre-mRNA splicing factors that play important roles in both constitutive and regulated splicing. Here, we describe one member of the family, which we call SRp38, with unexpected properties. Unlike other SR proteins, SRp38 cannot activate splicing and is essentially inactive in splicing assays. However, dephosphorylation converts SRp38 to a potent, general repr...
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ژورنال
عنوان ژورنال: Nature Structural & Molecular Biology
سال: 2008
ISSN: 1545-9993,1545-9985
DOI: 10.1038/nsmb.1485