Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*

Pearson, Gray W.; Robinson, Fred L.; Gibson, Tara Beers; Xu, Bing; Karandikar, Mahesh; Berman, Kevin; Cobb, Melanie H.

doi:10.1210/edrv.22.2.0428

Cited by 2,405 publications

(1,681 citation statements)

References 439 publications

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“…Unlike the p38 whose activity is mostly controlled by stress and proinflammatory stimuli [5], the activation of the ERK is controlled primarily by mitogens which signal through receptors involved in cell growth, proliferation and differentiation including Gprotein coupled receptors, receptor tyrosine kinases, Integrins, and Ion Channels [14,15]. Surprisingly, the CpG stimulation down-regulated the levels of p-ERK at all sampling time points indicating that this process is not transient but it is both fast and relatively long-lasting (Fig.…”

Section: Time Course Of the Mk2 P38 Erk And Mkk3/6 Phosphorylation mentioning

confidence: 99%

CpG- and LPS-activated MAPK signaling in in vitro cultured salmon (Salmo salar) mononuclear phagocytes

Iliev

Hansen

Jørgensen

et al. 2013

Fish & Shellfish Immunology

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Section: Time Course Of the Mk2 P38 Erk And Mkk3/6 Phosphorylation mentioning

confidence: 99%

CpG- and LPS-activated MAPK signaling in in vitro cultured salmon (Salmo salar) mononuclear phagocytes

Iliev

Hansen

Jørgensen

et al. 2013

Fish & Shellfish Immunology

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“…Several distinct families of MAPK signaling pathways have been described in metazoans: the extracellular signal-regulated kinase (ERK) cascade, the stress-activated protein kinase/c-Jun N-terminal kinase (hereafter referred to as SAPK) cascade and the p38 cascade (Widmann et al, 1999). In cultured cells, proliferation and differentiation signals preferentially activate ERKs, while inflammatory cytokines and stresses strongly elevate endogenous SAPK and p38 activities (Pearson et al, 2001). Thus it appears that both SAPK and p38 have roles in the physiological response to multiple types of stress.…”

Section: Introductionmentioning

confidence: 99%

Immediate-early gene induction by the stresses anisomycin and arsenite in human osteosarcoma cells involves MAPK cascade signaling to Elk-1, CREB and SRF

et al. 2003

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Cellular stress activates multiple mitogen-activated protein kinase (MAPK) cascades and immediate-early gene (IEG) transcription. To address how these events are linked, we investigated the endogenous signaling/transcription factor network driving IEG activation by arsenite and anisomycin in the human osteosarcoma cell line HOS/TE-85. Induction of IEG transcription by both stresses corresponded temporally with the phosphorylation of the regulatory factors Elk-1 and cAMP response element-binding protein (CREB), along with activation of the extracellular signal-regulated kinase (ERK), stressactivated protein kinase (SAPK) and p38 MAPK cascades. To assess the role of the different cascades, they were selectively inhibited with PD98059, SP600125 and SB203580, respectively. This implicated all three cascades in Elk-1 phosphorylation after arsenite treatment, whereas ERK and SAPK inhibition diminished this, and IEG mRNA levels, downstream of anisomycin. SB blocked phosphorylation of both serum response factor (SRF) and CREB, and strongly reduced IEG activation by both stresses. Combining PD with SB further reduced arsenite induction of IEG transcription. Thus, all three MAPK cascades mediate anisomycin-and arseniteinduced signaling to IEG promoters in HOS cells through the differential targeting of Elk-1, SRF and CREB.

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“…Activated Raf phosphorylates Mek, which in turn phosphorylates and activates the mitogen-activated protein kinase (MAPK), extracellular regulated kinase (Erk) 1/2. Erk dimerizes and translocates to the nucleus where it stimulates the activity of transcription factors, including Elk-1 (Pearson et al, 2001).…”

Section: Introductionmentioning

confidence: 99%

Akt negatively regulates translation of the ternary complex factor Elk-1

Figueroa

Vojtek

2003

Oncogene

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Cross-talk between signaling pathways plays an important role in regulation of cell growth, differentiation, survival, and death. Here, we show that Akt regulates the Elk-1 transcription factor, independent of its negative regulation of Raf kinases. Using a constitutively active Mek1 to bypass the regulation of Raf by Akt, we find that the Elk-1 and Sap1a proteins are dramatically decreased in the presence of activated Akt. Akt catalytic activity is required. Also, Mek-dependent activation of a TCF (Elk-1/Sap-1a)-dependent c-fos reporter is decreased by activated Akt. Neither the level of Elk-1 mRNA nor the stability of the Elk-1 protein is altered by activated Akt. Instead, the rate of incorporation of labeled methionine into Elk-1 protein is decreased in the presence of Akt. In addition, the level of the Elk-1 protein but not GFP is significantly decreased in the presence of activated Akt, when GFP is expressed from an IRES element in a bicistronic message with Elk-1. We conclude that Akt negatively regulates translation of the Elk-1 mRNA. A coding region determinant that maps within the first 279 nts of the Elk-1 message is necessary and sufficient for Akt-mediated regulation of Elk-1.

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Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*

Cited by 2,405 publications

References 439 publications

CpG- and LPS-activated MAPK signaling in in vitro cultured salmon (Salmo salar) mononuclear phagocytes

CpG- and LPS-activated MAPK signaling in in vitro cultured salmon (Salmo salar) mononuclear phagocytes

Immediate-early gene induction by the stresses anisomycin and arsenite in human osteosarcoma cells involves MAPK cascade signaling to Elk-1, CREB and SRF

Akt negatively regulates translation of the ternary complex factor Elk-1

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