The SR protein SRp38 represses splicing in M phase cells - PubMed

The SR protein SRp38 represses splicing in M phase cells

Chanseok Shin et al. Cell. 2002.

Free article

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.

Similar articles

• Multiple properties of the splicing repressor SRp38 distinguish it from typical SR proteins.

  Shin C, Kleiman FE, Manley JL. Shin C, et al. Mol Cell Biol. 2005 Sep;25(18):8334-43. doi: 10.1128/MCB.25.18.8334-8343.2005. Mol Cell Biol. 2005. PMID: 16135820 Free PMC article.

• A complex signaling pathway regulates SRp38 phosphorylation and pre-mRNA splicing in response to heat shock.

  Shi Y, Manley JL. Shi Y, et al. Mol Cell. 2007 Oct 12;28(1):79-90. doi: 10.1016/j.molcel.2007.08.028. Mol Cell. 2007. PMID: 17936706

• Dephosphorylated SRp38 acts as a splicing repressor in response to heat shock.

  Shin C, Feng Y, Manley JL. Shin C, et al. Nature. 2004 Feb 5;427(6974):553-8. doi: 10.1038/nature02288. Nature. 2004. PMID: 14765198

• Splicing regulation: the cell cycle connection.

  Blencowe BJ. Blencowe BJ. Curr Biol. 2003 Feb 18;13(4):R149-51. doi: 10.1016/s0960-9822(03)00079-4. Curr Biol. 2003. PMID: 12593819 Review.

• Cellular stress and RNA splicing.

  Biamonti G, Caceres JF. Biamonti G, et al. Trends Biochem Sci. 2009 Mar;34(3):146-53. doi: 10.1016/j.tibs.2008.11.004. Epub 2009 Feb 7. Trends Biochem Sci. 2009. PMID: 19208481 Review.

Cited by

• Nuclear speckle-associated protein Pnn/DRS binds to the transcriptional corepressor CtBP and relieves CtBP-mediated repression of the E-cadherin gene.

  Alpatov R, Munguba GC, Caton P, Joo JH, Shi Y, Shi Y, Hunt ME, Sugrue SP. Alpatov R, et al. Mol Cell Biol. 2004 Dec;24(23):10223-35. doi: 10.1128/MCB.24.23.10223-10235.2004. Mol Cell Biol. 2004. PMID: 15542832 Free PMC article.

• U1-independent pre-mRNA splicing contributes to the regulation of alternative splicing.

  Fukumura K, Taniguchi I, Sakamoto H, Ohno M, Inoue K. Fukumura K, et al. Nucleic Acids Res. 2009 Apr;37(6):1907-14. doi: 10.1093/nar/gkp050. Epub 2009 Feb 3. Nucleic Acids Res. 2009. PMID: 19190090 Free PMC article.

• Regulating the regulator: a survey of mechanisms from transcription to translation controlling expression of mammalian cell cycle kinase Aurora A.

  Cacioppo R, Lindon C. Cacioppo R, et al. Open Biol. 2022 Sep;12(9):220134. doi: 10.1098/rsob.220134. Epub 2022 Sep 7. Open Biol. 2022. PMID: 36067794 Free PMC article. Review.

• hnRNP I/PTB can antagonize the splicing repressor activity of SRp30c.

  Paradis C, Cloutier P, Shkreta L, Toutant J, Klarskov K, Chabot B. Paradis C, et al. RNA. 2007 Aug;13(8):1287-300. doi: 10.1261/rna.403607. Epub 2007 Jun 4. RNA. 2007. PMID: 17548433 Free PMC article.

• A novel SR-related protein is required for the second step of Pre-mRNA splicing.

  Cazalla D, Newton K, Cáceres JF. Cazalla D, et al. Mol Cell Biol. 2005 Apr;25(8):2969-80. doi: 10.1128/MCB.25.8.2969-2980.2005. Mol Cell Biol. 2005. PMID: 15798186 Free PMC article.

Publication types

MeSH terms

Substances

LinkOut - more resources

• Full Text Sources

  • Elsevier Science

• Molecular Biology Databases

  • GlyGen glycoinformatics resource

• Research Materials

  • NCI CPTC Antibody Characterization Program

• Miscellaneous

  • NCI CPTAC Assay Portal