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The Complex of p-Tyr42 RhoA and p-p65/RelA in Response to LPS Regulates the Expression of Phosphoglycerate Kinase 1.
Dogsom, Oyungerel; Hamza, Amir; Mahmud, Shohel; Min, Jung-Ki; Lee, Yoon-Beom; Park, Jae-Bong.
Afiliación
  • Dogsom O; Department of Biochemistry, Hallym University College of Medicine, Hallymdaehag-Gil 1, Chuncheon 24252, Kangwon-do, Republic of Korea.
  • Hamza A; Department of Biology, School of Bio-Medicine, Mongolian National University of Medical Sciences, Ulaanbaatar 14210, Mongolia.
  • Mahmud S; Department of Biochemistry, Hallym University College of Medicine, Hallymdaehag-Gil 1, Chuncheon 24252, Kangwon-do, Republic of Korea.
  • Min JK; Department of Biochemistry, Hallym University College of Medicine, Hallymdaehag-Gil 1, Chuncheon 24252, Kangwon-do, Republic of Korea.
  • Lee YB; National Institute of Biotechnology, Ganakbari, Ashulia, Savar 1349, Dhaka, Bangladesh.
  • Park JB; Department of Biochemistry, Hallym University College of Medicine, Hallymdaehag-Gil 1, Chuncheon 24252, Kangwon-do, Republic of Korea.
Antioxidants (Basel) ; 12(12)2023 Dec 08.
Article en En | MEDLINE | ID: mdl-38136210
ABSTRACT
Inflammation plays a crucial role in tumorigenesis, primarily mediated by NF-κB. RhoA GTPases are instrumental in regulating the activation of NF-κB. Specifically, the phosphorylation of Tyrosine 42 on RhoA ensures the activation of NF-κB by directly activating the IKKß associated with IKKγ (NEMO). This study aimed to uncover the molecular mechanism through which p-Tyrosine 42 RhoA, in conjunction with NF-κB, promotes tumorigenesis. Notably, we observed that p-Tyrosine 42 RhoA co-immunoprecipitated with the p-Ser 536 p65/RelA subunit in NF-κB in response to LPS. Moreover, both p-Tyrosine 42 RhoA and p-p65/RelA translocated to the nucleus, where they formed a protein complex associated with the promoter of phosphoglycerate kinase 1 (PGK1) and regulated the expression of PGK1. In addition, p-p65/RelA and p-Tyr42 RhoA co-immunoprecipitated with p300 histone acetyltransferase. Intriguingly, PGK1 exhibited an interaction with ß-catenin, PKM1 and PKM2. Of particular interest, si-PGK1 led to a reduction in the levels of ß-catenin and phosphorylated pyruvate dehydrogenase A1 (p-PDHA1). We also found that PGK1 phosphorylated ß-catenin at the Thr551 and Ser552 residues. These findings discovered that PGK1 may play a role in transcriptional regulation, alongside other transcription factors.
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Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Idioma: En Revista: Antioxidants (Basel) Año: 2023 Tipo del documento: Article

Texto completo: 1 Colección: 01-internacional Banco de datos: MEDLINE Idioma: En Revista: Antioxidants (Basel) Año: 2023 Tipo del documento: Article