Biomolecules | |
PTPIP51—A New RelA-tionship with the NFκB Signaling Pathway | |
Alexander Brobeil1  Fabian Kämmerer1  Claudia Tag1  Klaus Steger3  Stefan Gattenlöhner2  Monika Wimmer1  | |
[1] Institute of Anatomy and Cell Biology, Justus-Liebig-University, Gießen 35392, Germany; E-Mails:;Institute of Pathology, Justus-Liebig-University, Gießen 35392, Germany; E-Mail:;Department of Urology and Pediatric Urology, Justus-Liebig-University, Gießen 35392, Germany; E-Mail: | |
关键词: PTPIP51; NFκB; RelA; p65 subunit; | |
DOI : 10.3390/biom5020485 | |
来源: mdpi | |
【 摘 要 】
The present study shows a new connection of protein tyrosine phosphatase interacting protein 51 (PTPIP51) to the nuclear factor κB (NFκB) signalling pathway. PTPIP51 mRNA and protein expression is regulated by RelA. If bound to the PTPIP51 promoter, RelA repress the mRNA and protein expression of PTPIP51. The parallel treatment with pyrrolidine dithiocarbamate (PDTC) reversed the suppression of PTPIP51 protein expression induced by TNFα. Using the intensity correlation analysis PTPIP51 verified a co-localization with RelA, which is also regulated by TNFα administration. Moreover, the direct interaction of PTPIP51 and RelA was established using the DuoLink proximity ligation assay. IκBα, the known inhibitor of RelA, also interacted with PTPIP51. This hints to the fact that in un-stimulated conditions PTPIP51 forms a complex with RelA and IκBα. The PTPIP51/RelA/IκBα complex is modulated by TNFα. Interestingly, the impact on the mitogen activated protein kinase pathway was negligible except in highest TNFα concentration. Here, PTPIP51 and Raf-1 interactions were slightly repressed. The newly established relationship of PTPIP51 and the NFκB signaling pathway provides the basis for a possible therapeutic impact.
【 授权许可】
CC BY
© 2015 by the authors; licensee MDPI, Basel, Switzerland.
【 预 览 】
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