Regulation of protein kinase CK1alphaLS by dephosphorylation in response to hydrogen peroxide |
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Authors: | Bedri Shahinaz Cizek Stephanie M Rastarhuyeva Iryna Stone James R |
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Institution: | Department of Pathology, Massachusetts General Hospital, Harvard Medical School, Simches Research Building, Boston, MA 02114, USA. |
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Abstract: | Low levels of hydrogen peroxide (H(2)O(2)) are mitogenic to mammalian cells and stimulate the hyperphosphorylation of heterogeneous nuclear ribonucleoprotein C (hnRNP-C) by protein kinase CK1alpha. However, the mechanisms by which CK1alpha is regulated have been unclear. Here it is demonstrated that low levels of H(2)O(2) stimulate the rapid dephosphorylation of CK1alphaLS, a nuclear splice form of CK1alpha. Furthermore, it is demonstrated that either treatment of endothelial cells with H(2)O(2), or dephosphorylation of CK1alphaLS in vitro enhances the association of CK1alphaLS with hnRNP-C. In addition, dephosphorylation of CK1alphaLS in vitro enhances the kinase's ability to phosphorylate hnRNP-C. While CK1alpha appears to be present in all metazoans, analysis of CK1alpha genomic sequences from several species reveals that the alternatively spliced nuclear localizing L-insert is unique to vertebrates, as is the case for hnRNP-C. These observations indicate that CK1alphaLS and hnRNP-C represent conserved components of a vertebrate-specific H(2)O(2)-responsive nuclear signaling pathway. |
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Keywords: | Casein kinase Protein kinase CK1 Hydrogen peroxide Reactive oxygen species RNA binding proteins Protein kinases hnRNP-C Dephosphorylation Pre-mRNA processing |
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