Regulation of peroxiredoxin I activity by Cdc2-mediated phosphorylation
- Authors
- Chang T.-S.; Jeong W.; Choi S.Y.; Yu S.; Kang S.W.; Rhee S.G.
- Issue Date
- Jul-2002
- Publisher
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
- Citation
- Journal of Biological Chemistry, v.277, no.28, pp 25370 - 25376
- Pages
- 7
- Journal Title
- Journal of Biological Chemistry
- Volume
- 277
- Number
- 28
- Start Page
- 25370
- End Page
- 25376
- URI
- https://scholarworks.sookmyung.ac.kr/handle/2020.sw.sookmyung/16606
- DOI
- 10.1074/jbc.M110432200
- ISSN
- 0021-9258
1083-351X
- Abstract
- Hydrogen peroxide is implicated as an intracellular messenger in various cellular responses such as proliferation and differentiation. Peroxiredoxin (Prx) I is a member of the peroxiredoxin family of peroxidases and contains a consensus site (Thr90-Pro-Lys-Lys) for phosphorylation by cyclin-dependent kinases (CDKs). This protein has now been shown to be phosphorylated specifically on Thr90 by several CDKs, including Cdc2, in vitro. Phosphorylation of Prx I on Thr90 reduced the peroxidase activity of this protein by 80%. The phosphorylation of Prx I in HeLa cells was monitored with the use of antibodies specific for Prx I phosphorylated on Thr90. Immunoblot analysis with these antibodies of HeLa cells arrested at various stages of the cell cycle revealed that Prx I phosphorylation occurs in parallel with the activation of Cdc2; Prx I phosphorylation was thus marked during mitosis but virtually undetectable during interphase. Furthermore, when Cdc2 expression was reduced by RNA interference with cognate small interfering RNAs, Prx I phosphorylation was not observed in the cells synchronized in mitotic phase. The cytosolic location of Prx I likely prevents its interaction with activated CDKs until after the breakdown of the nuclear envelope during mitosis, when Cdc2 is the CDK that is most active. Phosphorylation of Prx I on Thr90 both in vitro and in vivo was blocked by roscovitine, an inhibitor of CDKs. These results suggest that Cdc2-mediated phosphorylation and inactivation of Prx I and the resulting intracellular accumulation of H2O2 might be important for progression of the cell cycle.
- Files in This Item
-
Go to Link
- Appears in
Collections - 이과대학 > 생명시스템학부 > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.