Abstract：
: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 repressor that inhibits splicing at an early step. To investigate the cellular function of SRp38, we examined its possible role in cell cycle control. We show first that splicing, like other steps in gene expression, is inhibited in extracts of mitotic cells. Strikingly, SRp38 was found to be dephosphorylated specifically in mitotic cells, and we show that dephosphorylated SRp38 is required for the observed splicing repression.
journal_name
Celljournal_title
Cellauthors
Shin C,Manley JLdoi
10.1016/s0092-8674(02)01038-3subject
Has Abstractpub_date
2002-11-01 00:00:00pages
407-17issue
3eissn
0092-8674issn
1097-4172pii
S0092867402010383journal_volume
111pub_type
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