The 90-kDa Ribosomal S6 Kinase (pp90rsk) Phosphorylates the N-terminal Regulatory Domain of IκBα and Stimulates Its Degradation in Vitro

Ghoda, Lucy; Lin, Xin; Greene, Warner C.

doi:10.1074/jbc.272.34.21281

Cited by 198 publications

(162 citation statements)

References 48 publications

(52 reference statements)

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“…Phosphorylation of IkB leads to its degradation, and the release and entry of NFkB into the nucleus where it can interact with promoter sequences (Rayet and Gelinas, 1999). RSK has been shown to phosphorylate IkBa on its S32/36 residue (Ghoda et al, 1997). Silencing YB-1 or PIK3CA decreased P-RSK (S380) as well as its downstream target P-IkBa (S32/36) (Figure 6d).…”

Section: Mda-mb-231mentioning

confidence: 97%

“…Activated AKT (Sutherland et al, 2005) or RSK (Stratford et al, 2008) phosphorylates YB-1 on its S102 site thereby allowing it to shuttle into the nucleus where it binds to the PIK3CA promoter to induce more p110a. This feedforward loop also causes an activation of signaling through RSK that enhances cellular invasion through phosphorylation of IkBa (Ghoda et al, 1997), allowing NFkB to enter into the nucleus where it can induce uPA production (Sliva et al, 2002). In closing, we determined for the first time that YB-1, which is a well-established oncogene for the development of mammary tumors, uses the induction of PIK3CA to bestow cellular invasion.…”

Section: Mda-mb-231mentioning

confidence: 98%

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The transcriptional induction of PIK3CA in tumor cells is dependent on the oncoprotein Y-box binding protein-1

et al. 2009

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Section: Mda-mb-231mentioning

confidence: 97%

Section: Mda-mb-231mentioning

confidence: 98%

The transcriptional induction of PIK3CA in tumor cells is dependent on the oncoprotein Y-box binding protein-1

et al. 2009

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“…For most inducers of NFkB activation, IkB phosphorylation occurs on serine residues S32 and S36, and a number of different kinases have been reported to phosphorylate IkB on these sites. These include Ik-kinase (IKK), NFkB-inducing kinase (NIK), double-stranded RNA-activated serine-threonine protein kinase (PKR) (reviewed in Janssen-Heininger et al, 2000), p90RSK (Ghoda et al, 1997), MEKK1 (Hirano et al, 1996;Meyer et al, 1996), and Akt (Madrid et al, 2001). Many of these kinases offer obvious points for cross talk with other signaling pathways known to be activated by oxidant injury.…”

Section: Nuclear Factor Kb (Nf Kb) Signalingmentioning

confidence: 99%

Cellular response to oxidative stress: Signaling for suicide and survival*

Martindale

Holbrook

2002

Journal Cellular Physiology

2,089

1,596

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Reactive oxygen species (ROS), whether produced endogenously as a consequence of normal cell functions or derived from external sources, pose a constant threat to cells living in an aerobic environment as they can result in severe damage to DNA, protein, and lipids. The importance of oxidative damage to the pathogenesis of many diseases as well as to degenerative processes of aging has becoming increasingly apparent over the past few years. Cells contain a number of antioxidant defenses to minimize fluctuations in ROS, but ROS generation often exceeds the cell's antioxidant capacity, resulting in a condition termed oxidative stress. Host survival depends upon the ability of cells and tissues to adapt to or resist the stress, and repair or remove damaged molecules or cells. Numerous stress response mechanisms have evolved for these purposes, and they are rapidly activated in response to oxidative insults. Some of the pathways are preferentially linked to enhanced survival, while others are more frequently associated with cell death. Still others have been implicated in both extremes depending on the particular circumstances. In this review, we discuss the various signaling pathways known to be activated in response to oxidative stress in mammalian cells, the mechanisms leading to their activation, and their roles in influencing cell survival. These pathways constitute important avenues for therapeutic interventions aimed at limiting oxidative damage or attenuating its sequelae. Published 2002 Wiley‐Liss, Inc.

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“…They are involved in the phosphorylation of histone H3 and remodeling of chromatin in response to epidermal growth factor (EGF) 25 and can regulate gene expression by phosphorylating transcription factors, including c-Fos, 26,27 cAMP-response element-binding protein (CREB), [28][29][30] CREB-binding protein, 31,32 estrogen receptor, 33 ATF4,34 NFATc4, 35 and NF-B/I B␣. 36,37 p90 Rsk2 was also reported to phosphorylate the p34 cdc2 inhibitory kinase Myt1 in frog oocytes, leading to activation of the cyclin-dependent kinase p34 cdc2 that then promotes cell-cycle progression of oocytes through the G2/M phase of meiosis. 38 Phosphorylation of the proapoptotic protein, Bcl-X L /Bcl-2-associated death promoter (Bad) by p90 Rsk2 suppresses Bad-mediated apoptosis in neurons.…”

Section: Introductionmentioning

confidence: 99%