RSK-B, a Novel Ribosomal S6 Kinase Family Member, Is a CREB Kinase under Dominant Control of p38α Mitogen-activated Protein Kinase (p38αMAPK)

Pierrat, Benoı̂t; Correia, Jean da Silva; Mary, Jean-Luc; Tomás-Zuber, Mar; Lesslauer, Werner

doi:10.1074/jbc.273.45.29661

Cited by 155 publications

(153 citation statements)

References 72 publications

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“…p38 regulated/activated kinase (PRAK) is a p38α and/or p38β activated kinase that shares 20-30% sequence identity to MK2 and is thought to regulate heat shock protein 27 (HSP27) [61]. Mitogen-and stress-activated protein kinase-1 (MSK1) can be directly activated by p38 and ERK, and may mediate activation of CREB [62][63][64]. p38 is also thought to regulate S phase activation of histone 2B (H2B) promoter through OCA-S, a component of p38 [65].…”

Section: Downstream Substrates Of P38 Group Map Kinases Protein Kinasmentioning

confidence: 99%

Activation and signaling of the p38 MAP kinase pathway

2005

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The family members of the mitogen-activated protein (MAP) kinases mediate a wide variety of cellular behaviors in response to extracellular stimuli. One of the four main sub-groups, the p38 group of MAP kinases, serve as a nexus for signal transduction and play a vital role in numerous biological processes. In this review, we highlight the known characteristics and components of the p38 pathway along with the mechanism and consequences of p38 activation. We focus on the role of p38 as a signal transduction mediator and examine the evidence linking p38 to inflammation, cell cycle, cell death, development, cell differentiation, senescence and tumorigenesis in specific cell types. Upstream and downstream components of p38 are described and questions remaining to be answered are posed. Finally, we propose several directions for future research on p38.

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Section: Downstream Substrates Of P38 Group Map Kinases Protein Kinasmentioning

confidence: 99%

Activation and signaling of the p38 MAP kinase pathway

2005

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“…Our previous results have pointed out the complexity of the MAP kinase signaling pathway, which is due to the fact that each individual MAP kinase can be activated by two or three upstream MAP2Ks and multiple MAP3Ks in Drosophila under different stimuli (Zhuang et al, 2006). Upon activation, p38 can phosphorylate and activate a number of transcription factors including ATF-2/ATF-7, CHOP/GADD153, Elk1, MEF2-C, Sap1 and CREB (Wang et al,1996;Raingeaud et al,1996;Han et al,1997;Iordanov et al,1997;Whitmarsh et al,1997;Shivers et al, 2010), and protein kinases such as MAPKAPK2, MNK, PRAK, MSK1 and RSK-B (Stokoe et al,1992;Fukunaga et al,1997;Waskiewicz et al,1997;New et al,1998;Deak et al,1998;Pierrat et al,1998), thus eliciting different cellular responses.…”

Section: Introductionmentioning

confidence: 99%

Caenorhabditis elegans mom-4 is required for the activation of the p38 MAPK signaling pathway in the response to Pseudomonas aeruginosa infection

Shi

Liu

et al. 2012

Protein Cell

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“…In cells, it has been shown that the activation of MSK by mitogens could be blocked by inhibitors of the ERK1/2 cascade, while the activation of MSK by cellular stress was blocked by inhibitors of p38α/β [14][15][16]. While both p38α and p38β can phosphorylate MSK1 in vitro [14], p38α appears to be the isoform responsible in vivo, as MSK1 activation is greatly reduced in cells from p38α, but not p38β, knockout mice [13,22].…”

Section: Introductionmentioning

confidence: 99%

“…MSKs are most closely related to the RSK (p90 ribosomal S6 kinase) family of kinases and, like RSK, MSKs contain two distinct kinase domains within a single polypeptide [14][15][16]. The N-terminal domain, which is thought to phosphorylate MSK substrates, is a member of the AGC-type kinases (protein kinase A/protein kinase G/protein kinase C-family kinases), while the C-terminal kinase domain is related to the calmodulin-dependent protein kinase family [17].…”

Section: Introductionmentioning

confidence: 99%

Identification of novel phosphorylation sites in MSK1 by precursor ion scanning MS

McCoy

Macdonald

Morrice

et al. 2007

Biochemical Journal

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MSK1 (mitogen-and stress-activated kinase 1) is a dual kinase domain protein that acts downstream of the ERK1/2 (extracellular-signal-regulated kinase 1/2) and p38 MAPK (mitogenactivated protein kinase) signalling pathways in cells. MSK1, and its related isoform MSK2, phosphorylate the transcription factors CREB (cAMP-response-element-binding protein) and ATF1 (activating transcription factor 1), and the chromatin proteins histone H3 and HMGN1 (high-mobility-group nucleosomalbinding protein 1) in response to either mitogenic stimulation or cellular stress. MSK1 activity is tightly regulated in cells, and activation requires the phosphorylation of MSK1 by either ERK1/2 or p38α. This results in activation of the C-terminal kinase domain, which then phosphorylates further sites in MSK1, leading to the activation of the N-terminal kinase domain and phosphorylation of substrates. Here, we use precursor ion scanning MS to identify five previously unknown sites in MSK1: Thr 630 , Ser 647 , Ser 657 , Ser 695 and Thr 700 . One of these sites, Thr 700 , was found to be a third site in MSK1 phosphorylated by the upstream kinases ERK1/2 and p38α. Mutation of Thr 700 resulted in an increased basal activity of MSK1, but this could be further increased by stimulation with PMA or UV-C radiation. Surprisingly, however, mutation of Thr 700 resulted in a dramatic loss of Thr 581 phosphorylation, a site essential for activity. Mutation of Thr 700 and Thr 581 to an alanine residue resulted in an inactive kinase, while mutation of both sites to an aspartic acid residue resulted in a kinase with a significant basal activity that could not be further stimulated. Together these results are consistent with a mechanism by which Thr 700 phosphorylation relieves the inhibition of MSK1 by a C-terminal autoinhibitory helix and helps induce a conformational shift that protects Thr 581 from dephosphorylation.

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RSK-B, a Novel Ribosomal S6 Kinase Family Member, Is a CREB Kinase under Dominant Control of p38α Mitogen-activated Protein Kinase (p38αMAPK)

Cited by 155 publications

References 72 publications

Activation and signaling of the p38 MAP kinase pathway

Activation and signaling of the p38 MAP kinase pathway

Caenorhabditis elegans mom-4 is required for the activation of the p38 MAPK signaling pathway in the response to Pseudomonas aeruginosa infection

Identification of novel phosphorylation sites in MSK1 by precursor ion scanning MS

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