Počet záznamů: 1  

Regulation of phosphosignaling pathways involved in transcription of cell cycle target genes by TRH receptor activation in GH1 cells

  1. 1.
    SYSNO ASEP0580215
    Druh ASEPJ - Článek v odborném periodiku
    Zařazení RIVJ - Článek v odborném periodiku
    Poddruh JČlánek ve WOS
    NázevRegulation of phosphosignaling pathways involved in transcription of cell cycle target genes by TRH receptor activation in GH1 cells
    Tvůrce(i) Drastichová, Z. (CZ)
    Trubačová, Radka (FGU-C)
    Novotný, J. (CZ)
    Číslo článku115830
    Zdroj.dok.Biomedicine & Pharmacotherapy. - : Elsevier - ISSN 0753-3322
    Roč. 168, Dec (2023)
    Poč.str.18 s.
    Jazyk dok.eng - angličtina
    Země vyd.NL - Nizozemsko
    Klíč. slovaβ-arrestin2 ; cell cycle ; phosphosignaling ; Taltirelin ; Thyrotropin-releasing hormone
    Obor OECDBiochemistry and molecular biology
    Způsob publikováníOpen access
    Institucionální podporaFGU-C - RVO:67985823
    UT WOS001113579600001
    EID SCOPUS85175557838
    DOI10.1016/j.biopha.2023.115830
    AnotaceThyrotropin-releasing hormone (TRH) is known to activate several cellular signaling pathway, but the activation of the TRH receptor (TRH-R) has not been reported to regulate gene transcription. The aim of this study was to identify phosphosignaling pathways and phosphoprotein complexes associated with gene transcription in GH1 pituitary cells treated with TRH or its analog, taltirelin (TAL), using label-free bottom-up mass spectrometry-based proteomics. Our detailed analysis provided insight into the mechanism through which TRH-R activation may regulate the transcription of genes related to the cell cycle and proliferation. It involves control of the signaling pathways for β-catenin/Tcf, Notch/RBPJ, p53/p21/Rbl2/E2F, Myc, and YY1/Rb1/E2F through phosphorylation and dephosphorylation of their key components. In many instances, the phosphorylation patterns of differentially phosphorylated phosphoproteins in TRH- or TAL-treated cells were identical or displayed a similar trend in phosphorylation. However, some phosphoproteins, especially components of the Wnt/β-catenin/Tcf and YY1/Rb1/E2F pathways, exhibited different phosphorylation patterns in TRH- and TAL-treated cells. This supports the notion that TRH and TAL may act, at least in part, as biased agonists. Additionally, the deficiency of β-arrestin2 resulted in a reduced number of alterations in phosphorylation, highlighting the critical role of β-arrestin2 in the signal transduction from TRH-R in the plasma membrane to transcription factors in the nucleus.
    PracovištěFyziologický ústav
    KontaktLucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400
    Rok sběru2024
    Elektronická adresahttps://doi.org/10.1016/j.biopha.2023.115830
Počet záznamů: 1  

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