Phosphorylation Status of Nuclear Ribosomal Protein S3 Is Reciprocally Regulated by Protein Kinase C delta and Protein Phosphatase 2A
DC Field | Value | Language |
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dc.contributor.author | Kim, Tae-Sung | - |
dc.contributor.author | Kim, Hag Dong | - |
dc.contributor.author | Shin, Hyun-Seock | - |
dc.contributor.author | Kim, Joon | - |
dc.date.accessioned | 2021-09-08T14:51:26Z | - |
dc.date.available | 2021-09-08T14:51:26Z | - |
dc.date.created | 2021-06-10 | - |
dc.date.issued | 2009-08-07 | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/119502 | - |
dc.description.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. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC | - |
dc.subject | TUMOR-SUPPRESSOR PP2A | - |
dc.subject | MEDIATED PHOSPHORYLATION | - |
dc.subject | FUNCTIONAL INTERACTION | - |
dc.subject | GROWTH-FACTOR | - |
dc.subject | DNA-DAMAGE | - |
dc.subject | B-SUBUNITS | - |
dc.subject | IDENTIFICATION | - |
dc.subject | COMPLEXES | - |
dc.subject | CELLS | - |
dc.subject | ERK | - |
dc.title | Phosphorylation Status of Nuclear Ribosomal Protein S3 Is Reciprocally Regulated by Protein Kinase C delta and Protein Phosphatase 2A | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Tae-Sung | - |
dc.contributor.affiliatedAuthor | Kim, Joon | - |
dc.identifier.doi | 10.1074/jbc.M109.018168 | - |
dc.identifier.scopusid | 2-s2.0-69249122868 | - |
dc.identifier.wosid | 000268564400013 | - |
dc.identifier.bibliographicCitation | JOURNAL OF BIOLOGICAL CHEMISTRY, v.284, no.32, pp.21201 - 21208 | - |
dc.relation.isPartOf | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.title | JOURNAL OF BIOLOGICAL CHEMISTRY | - |
dc.citation.volume | 284 | - |
dc.citation.number | 32 | - |
dc.citation.startPage | 21201 | - |
dc.citation.endPage | 21208 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.subject.keywordPlus | TUMOR-SUPPRESSOR PP2A | - |
dc.subject.keywordPlus | MEDIATED PHOSPHORYLATION | - |
dc.subject.keywordPlus | FUNCTIONAL INTERACTION | - |
dc.subject.keywordPlus | GROWTH-FACTOR | - |
dc.subject.keywordPlus | DNA-DAMAGE | - |
dc.subject.keywordPlus | B-SUBUNITS | - |
dc.subject.keywordPlus | IDENTIFICATION | - |
dc.subject.keywordPlus | COMPLEXES | - |
dc.subject.keywordPlus | CELLS | - |
dc.subject.keywordPlus | ERK | - |
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