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Phosphorylation Status of Nuclear Ribosomal Protein S3 Is Reciprocally Regulated by Protein Kinase C delta and Protein Phosphatase 2A

Authors
Kim, Tae-SungKim, Hag DongShin, Hyun-SeockKim, Joon
Issue Date
7-8월-2009
Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
Citation
JOURNAL OF BIOLOGICAL CHEMISTRY, v.284, no.32, pp.21201 - 21208
Indexed
SCIE
SCOPUS
Journal Title
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume
284
Number
32
Start Page
21201
End Page
21208
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/119502
DOI
10.1074/jbc.M109.018168
ISSN
0021-9258
Abstract
It has been shown previously that ribosomal protein S3 (rpS3) has an endonuclease activity, which is increased by protein kinase C delta (PKC delta)-dependent phosphorylation. However, the reciprocal mechanism for rpS3 dephosphorylation is not known. In this study, we examined phosphatases involved in rpS3 dephosphorylation, and we determined that rpS3 is specifically dephosphorylated by protein phosphatase 2A (PP2A). By immunoprecipitation assay, rpS3 only interacted with PP2Ac but not with protein phosphatase 1. The interaction between rpS3 and PP2Ac occurred only in the nuclear fraction. Moreover, the PP2Ac association with rpS3 was identified in cells transfected with wild-type rpS3 but not with mutant rpS3 lacking PKC delta phosphorylation sites. PP2A inhibition using okadaic acid induced rpS3 phosphorylation. The level of phosphorylated rpS3 in cells was decreased by the overexpression of PP2Ac and was increased by the down-regulation of PP2Ac. Taken together, these results suggest that oxidative stress regulates the phosphorylation status of nonribosomal rpS3 by both activating PKC delta and blocking the PP2A interaction with rpS3.
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