TPA-induced cell transformation provokes a complex formation between Pin1 and 90 kDa ribosomal protein S6 kinase 2
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Cho, Young Sik | - |
dc.contributor.author | Park, Seung Yeon | - |
dc.contributor.author | Kim, Dong Joon | - |
dc.contributor.author | Lee, Sang-Han | - |
dc.contributor.author | Woo, Kee-Min | - |
dc.contributor.author | Lee, Kyung-Ae | - |
dc.contributor.author | Lee, Yoon-Jin | - |
dc.contributor.author | Cho, Yong-Yeon | - |
dc.contributor.author | Shim, Jung-Hyun | - |
dc.date.accessioned | 2021-08-12T02:47:30Z | - |
dc.date.available | 2021-08-12T02:47:30Z | - |
dc.date.issued | 2012-08 | - |
dc.identifier.issn | 0300-8177 | - |
dc.identifier.issn | 1573-4919 | - |
dc.identifier.uri | https://scholarworks.bwise.kr/sch/handle/2021.sw.sch/14982 | - |
dc.description.abstract | Post-translational modification of peptidyl cis/trans prolyl isomerase Pin1 is crucial in regulation of gene stability. Pin1 phosphorylation at Ser(16) has been regarded as a marker for Pin1 isomerase activity and introduction of phosphorylation on Ser/Thr-Pro of substrate proteins is prerequisite for its binding activity with Pin1 and subsequent isomerization. Here, we found that 90 kDa ribosomal protein S6 kinase 2 (RSK2) could form a physical complex with Pin1, leading to phosphorylation of Pin1 at Ser(16) ex vivo and in vitro respectively. Intriguingly, Pin1(+/+) mouse embryonic fibroblasts (MEFs) exhibited significantly an increase in 12-O-tetradecanoylphorbol-13-acetate (TPA)-induced RSK2 phosphorylation with a marginal Pin1 phosphorylation compared with Pin1(-/-) MEFs. Moreover, TPA-induced Ser(16) Pin1 phosphorylation as well as RSK2 phosphorylation was considerably profound in RSK+/+ MEFs but not in RSK-/- MEFs. Consequently, knockdown of Pin1 using shRNA-Pin1 suppressed TPA-induced cell transformation in JB6 CI41 cells. Overall, these results indicate that Pin1 plays a critical role in TPA-induced tumorigenesis plausibly via physical interaction with RSK2 and reciprocal phosphorylation, therefore suggesting a potential therapeutic target for cancer treatment. | - |
dc.format.extent | 8 | - |
dc.language | 영어 | - |
dc.language.iso | ENG | - |
dc.publisher | Kluwer Academic/Plenum Publishers | - |
dc.title | TPA-induced cell transformation provokes a complex formation between Pin1 and 90 kDa ribosomal protein S6 kinase 2 | - |
dc.type | Article | - |
dc.publisher.location | 네델란드 | - |
dc.identifier.doi | 10.1007/s11010-012-1322-y | - |
dc.identifier.scopusid | 2-s2.0-84863456586 | - |
dc.identifier.wosid | 000305683100010 | - |
dc.identifier.bibliographicCitation | Molecular and Cellular Biochemistry, v.367, no.1-2, pp 85 - 92 | - |
dc.citation.title | Molecular and Cellular Biochemistry | - |
dc.citation.volume | 367 | - |
dc.citation.number | 1-2 | - |
dc.citation.startPage | 85 | - |
dc.citation.endPage | 92 | - |
dc.type.docType | Article | - |
dc.description.isOpenAccess | N | - |
dc.description.journalRegisteredClass | sci | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordPlus | PROLYL ISOMERASE PIN1 | - |
dc.subject.keywordPlus | C-JUN | - |
dc.subject.keywordPlus | REGULATORY MECHANISM | - |
dc.subject.keywordPlus | BREAST-CANCER | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | ISOMERIZATION | - |
dc.subject.keywordPlus | PHOSPHOPROTEINS | - |
dc.subject.keywordPlus | PHOSPHOSERINE | - |
dc.subject.keywordPlus | STABILITY | - |
dc.subject.keywordAuthor | Ribosomal S6 kinase 2 | - |
dc.subject.keywordAuthor | Peptidyl cis/trans prolyl isomerase | - |
dc.subject.keywordAuthor | Tumorigenesis | - |
dc.subject.keywordAuthor | 12-O-tetradecanoylphorbol-13-acetate | - |
dc.subject.keywordAuthor | Post-translational modification | - |
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.
(31538) 22, Soonchunhyang-ro, Asan-si, Chungcheongnam-do, Republic of Korea+82-41-530-1114
COPYRIGHT 2021 by SOONCHUNHYANG UNIVERSITY ALL RIGHTS RESERVED.
Certain data included herein are derived from the © Web of Science of Clarivate Analytics. All rights reserved.
You may not copy or re-distribute this material in whole or in part without the prior written consent of Clarivate Analytics.