Regulation of protein kinase CK1αLS by dephosphorylation in response to hydrogen peroxide

Shahinaz Bedri, Stephanie M. Cizek, Iryna Rastarhuyeva, James R. Stone

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

Low levels of hydrogen peroxide (H2O2) are mitogenic to mammalian cells and stimulate the hyperphosphorylation of heterogeneous nuclear ribonucleoprotein C (hnRNP-C) by protein kinase CK1α. However, the mechanisms by which CK1α is regulated have been unclear. Here it is demonstrated that low levels of H2O2 stimulate the rapid dephosphorylation of CK1αLS, a nuclear splice form of CK1α. Furthermore, it is demonstrated that either treatment of endothelial cells with H2O2, or dephosphorylation of CK1αLS in vitro enhances the association of CK1αLS with hnRNP-C. In addition, dephosphorylation of CK1αLS in vitro enhances the kinase's ability to phosphorylate hnRNP-C. While CK1α appears to be present in all metazoans, analysis of CK1α 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 CK1αLS and hnRNP-C represent conserved components of a vertebrate-specific H2O2-responsive nuclear signaling pathway.

Original languageEnglish
Pages (from-to)242-249
Number of pages8
JournalArchives of Biochemistry and Biophysics
Volume466
Issue number2
DOIs
Publication statusPublished - 15 Oct 2007
Externally publishedYes

Fingerprint

Heterogeneous-Nuclear Ribonucleoproteins
Heterogeneous-Nuclear Ribonucleoprotein Group C
Protein Kinases
Hydrogen Peroxide
Vertebrates
Casein Kinase I
Endothelial cells
Phosphotransferases
Endothelial Cells
Cells
In Vitro Techniques

Keywords

  • Casein kinase
  • Dephosphorylation
  • hnRNP-C
  • Hydrogen peroxide
  • Pre-mRNA processing
  • Protein kinase CK1
  • Protein kinases
  • Reactive oxygen species
  • RNA binding proteins

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology

Cite this

Regulation of protein kinase CK1αLS by dephosphorylation in response to hydrogen peroxide. / Bedri, Shahinaz; Cizek, Stephanie M.; Rastarhuyeva, Iryna; Stone, James R.

In: Archives of Biochemistry and Biophysics, Vol. 466, No. 2, 15.10.2007, p. 242-249.

Research output: Contribution to journalArticle

Bedri, Shahinaz ; Cizek, Stephanie M. ; Rastarhuyeva, Iryna ; Stone, James R. / Regulation of protein kinase CK1αLS by dephosphorylation in response to hydrogen peroxide. In: Archives of Biochemistry and Biophysics. 2007 ; Vol. 466, No. 2. pp. 242-249.
@article{276f9aca227c4381a98c8d837043dd16,
title = "Regulation of protein kinase CK1αLS by dephosphorylation in response to hydrogen peroxide",
abstract = "Low levels of hydrogen peroxide (H2O2) are mitogenic to mammalian cells and stimulate the hyperphosphorylation of heterogeneous nuclear ribonucleoprotein C (hnRNP-C) by protein kinase CK1α. However, the mechanisms by which CK1α is regulated have been unclear. Here it is demonstrated that low levels of H2O2 stimulate the rapid dephosphorylation of CK1αLS, a nuclear splice form of CK1α. Furthermore, it is demonstrated that either treatment of endothelial cells with H2O2, or dephosphorylation of CK1αLS in vitro enhances the association of CK1αLS with hnRNP-C. In addition, dephosphorylation of CK1αLS in vitro enhances the kinase's ability to phosphorylate hnRNP-C. While CK1α appears to be present in all metazoans, analysis of CK1α 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 CK1αLS and hnRNP-C represent conserved components of a vertebrate-specific H2O2-responsive nuclear signaling pathway.",
keywords = "Casein kinase, Dephosphorylation, hnRNP-C, Hydrogen peroxide, Pre-mRNA processing, Protein kinase CK1, Protein kinases, Reactive oxygen species, RNA binding proteins",
author = "Shahinaz Bedri and Cizek, {Stephanie M.} and Iryna Rastarhuyeva and Stone, {James R.}",
year = "2007",
month = "10",
day = "15",
doi = "10.1016/j.abb.2007.06.010",
language = "English",
volume = "466",
pages = "242--249",
journal = "Archives of Biochemistry and Biophysics",
issn = "0003-9861",
publisher = "Academic Press Inc.",
number = "2",

}

TY - JOUR

T1 - Regulation of protein kinase CK1αLS by dephosphorylation in response to hydrogen peroxide

AU - Bedri, Shahinaz

AU - Cizek, Stephanie M.

AU - Rastarhuyeva, Iryna

AU - Stone, James R.

PY - 2007/10/15

Y1 - 2007/10/15

N2 - Low levels of hydrogen peroxide (H2O2) are mitogenic to mammalian cells and stimulate the hyperphosphorylation of heterogeneous nuclear ribonucleoprotein C (hnRNP-C) by protein kinase CK1α. However, the mechanisms by which CK1α is regulated have been unclear. Here it is demonstrated that low levels of H2O2 stimulate the rapid dephosphorylation of CK1αLS, a nuclear splice form of CK1α. Furthermore, it is demonstrated that either treatment of endothelial cells with H2O2, or dephosphorylation of CK1αLS in vitro enhances the association of CK1αLS with hnRNP-C. In addition, dephosphorylation of CK1αLS in vitro enhances the kinase's ability to phosphorylate hnRNP-C. While CK1α appears to be present in all metazoans, analysis of CK1α 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 CK1αLS and hnRNP-C represent conserved components of a vertebrate-specific H2O2-responsive nuclear signaling pathway.

AB - Low levels of hydrogen peroxide (H2O2) are mitogenic to mammalian cells and stimulate the hyperphosphorylation of heterogeneous nuclear ribonucleoprotein C (hnRNP-C) by protein kinase CK1α. However, the mechanisms by which CK1α is regulated have been unclear. Here it is demonstrated that low levels of H2O2 stimulate the rapid dephosphorylation of CK1αLS, a nuclear splice form of CK1α. Furthermore, it is demonstrated that either treatment of endothelial cells with H2O2, or dephosphorylation of CK1αLS in vitro enhances the association of CK1αLS with hnRNP-C. In addition, dephosphorylation of CK1αLS in vitro enhances the kinase's ability to phosphorylate hnRNP-C. While CK1α appears to be present in all metazoans, analysis of CK1α 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 CK1αLS and hnRNP-C represent conserved components of a vertebrate-specific H2O2-responsive nuclear signaling pathway.

KW - Casein kinase

KW - Dephosphorylation

KW - hnRNP-C

KW - Hydrogen peroxide

KW - Pre-mRNA processing

KW - Protein kinase CK1

KW - Protein kinases

KW - Reactive oxygen species

KW - RNA binding proteins

UR - http://www.scopus.com/inward/record.url?scp=34648814417&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34648814417&partnerID=8YFLogxK

U2 - 10.1016/j.abb.2007.06.010

DO - 10.1016/j.abb.2007.06.010

M3 - Article

C2 - 17626781

AN - SCOPUS:34648814417

VL - 466

SP - 242

EP - 249

JO - Archives of Biochemistry and Biophysics

JF - Archives of Biochemistry and Biophysics

SN - 0003-9861

IS - 2

ER -