| First Author | Díaz-Mora E | Year | 2023 |
| Journal | Front Cell Dev Biol | Volume | 11 |
| Pages | 1083033 | PubMed ID | 36846591 |
| Mgi Jnum | J:343362 | Mgi Id | MGI:7440594 |
| Doi | 10.3389/fcell.2023.1083033 | Citation | Diaz-Mora E, et al. (2023) p38delta controls Mitogen- and Stress-activated Kinase-1 (MSK1) function in response to toll-like receptor activation in macrophages. Front Cell Dev Biol 11:1083033 |
| abstractText | Mitogen- and Stress-activated Kinase (MSK) 1 is a nuclear protein, activated by p38alpha Mitogen-Activated Kinase (MAPK) and extracellular signal-regulated kinase (ERK1/2), that modulate the production of certain cytokines in macrophages. Using knockout cells and specific kinase inhibitors, we show that, besides p38alpha and ERK1/2, another p38MAPK, p38delta, mediates MSK phosphorylation and activation, in LPS-stimulated macrophages. Additionally, recombinant MSK1 was phosphorylated and activated by recombinant p38delta, to the same extent than by p38alpha, in in vitro experiments. Moreover, the phosphorylation of the transcription factors CREB and ATF1, that are MSK physiological substrates, and the expression of the CREB-dependent gene encoding DUSP1, were impaired in p38delta-deficient macrophages. Also, the transcription of IL-1Ra mRNA, that is MSK-dependent, was reduced. Our results indicate that MSK activation can be one possible mechanism by which p38delta regulates the production of a variety of inflammatory molecules involved in immune innate response. |
