Ras-induced serine phosphorylation of the focal adhesion protein paxillin is mediated by the Raf-->MEK-->ERK pathway.

@article{Woodrow2003RasinducedSP,
  title={Ras-induced serine phosphorylation of the focal adhesion protein paxillin is mediated by the Raf-->MEK-->ERK pathway.},
  author={Melissa Woodrow and Douglas B Woods and Holly M. Cherwinski and David Stokoe and Martin McMahon},
  journal={Experimental cell research},
  year={2003},
  volume={287 2},
  pages={
          325-38
        }
}
The Rho GTPase Effector ROCK Regulates Cyclin A, Cyclin D1, and p27Kip1 Levels by Distinct Mechanisms
TLDR
Using a conditionally activated ROCK-estrogen receptor fusion protein, it is found that ROCK activation is sufficient to stimulate G1/S cell cycle progression in NIH 3T3 mouse fibroblasts and revealed that ROCK acts via independent pathways to alter the levels of cell cycle regulatory proteins.
Serine phosphorylation regulates paxillin turnover during cell migration
TLDR
The data demonstrate for the first time that serine-regulated degradation of paxillin plays a key role in the modulation of membrane dynamics and consequently, in the control of cell motility.
β‐arrestin 2‐dependent activation of ERK1/2 is required for ADP‐induced paxillin phosphorylation at Ser83 and microglia chemotaxis
TLDR
Examining the role of ERK1/2 activation in ADP‐induced microglia chemotaxis revealed that the phosphorylation of paxillin at Tyr31 by c‐Src appears to be involved in adhesion formation upon ADP stimulation while Ser83 required for adhesion disassembly.
B-Raf Regulation of Integrin α4β1-mediated Resistance to Shear Stress through Changes in Cell Spreading and Cytoskeletal Association in T Cells*
TLDR
A novel role for B-Raf is demonstrated in the selective regulation of α4β1 integrin-mediated adhesion and this association suggests new therapeutic targets in T cells and indicates potential off-target effects of sorafenib.
Paxillin Regulates Steroid-triggered Meiotic Resumption in Oocytes by Enhancing an All-or-None Positive Feedback Kinase Loop*
TLDR
Oocyte maturation is triggered by steroids in a transcription-independent fashion that involves an unusual positive feedback loop whereby MOS activates MEK1, which in turn activates ERK2, which acts back on MOS to enhance its expression and amplify the kinase signaling cascade.
Paxillin Regulates Androgen- and Epidermal Growth Factor-induced MAPK Signaling and Cell Proliferation in Prostate Cancer Cells*
TLDR
It is shown that in LnCAP cells DHT functions as a growth factor that indirectly activates the EGF-receptor via androgen receptor binding and matrix metalloproteinase-mediated release of EGFR ligands, suggesting that paxillin may regulate prostate cancer proliferation by serving as a liaison between extra-nuclear kinase signaling and intra-nuclear transcriptional signals.
EGF‐induced ERK‐activation downstream of FAK requires rac1‐NADPH oxidase
TLDR
The data suggest that Rac1 through NADPH oxidase is part of the signaling pathway constituted by FAK, Rac1, and ERK that regulates focal adhesion disassembly during cell spreading, and this role is proposed as a modulator of the FAK autophosphorylation site.
Paxillin: a crossroad in pathological cell migration
TLDR
Upon integrin engagement with extracellular matrix, paxillin is phosphorylated at Tyr31, Tyr118, Ser188, and Ser190, activating numerous signaling cascades which promote cell migration, indicating that the regulation of adhesion dynamics is under the control of a complex display of signaling mechanisms.
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References

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MEK Mediates v-Src-induced Disruption of the Actin Cytoskeleton via Inactivation of the Rho-ROCK-LIM Kinase Pathway*
TLDR
MEK is established as an effector of v-Src-induced cytoskeleton disruption, participating in v- SRC-induced antagonism of the cellular function of Rho, thereby uncoupling Rho from stress fiber formation.
Hepatocyte Growth Factor Induces ERK-dependent Paxillin Phosphorylation and Regulates Paxillin-Focal Adhesion Kinase Association*
TLDR
Data suggest that HGF can induce serine/threonine phosphorylation of paxillin most probably mediated directly by ERK, resulting in the recruitment and activation of FAK and subsequent enhancement of cell spreading and adhesion.
Adhesion of fibroblasts to fibronectin stimulates both serine and tyrosine phosphorylation of paxillin.
TLDR
Findings support a role for both tyrosine and serine kinases in the signal transduction pathway linking integrin activation to paxillin phosphorylation.
Epidermal growth factor stimulates serine/threonine phosphorylation of the focal adhesion protein paxillin in a MEK‐dependent manner in normal rat kidney cells
TLDR
Paxillin is identified as a component EGF signaling in renal epithelial cells and members of the MAP kinase pathway as critical regulators of paxillin serine/threonine phosphorylation are implicate.
Post-transcriptional down-regulation of ROCKI/Rho-kinase through an MEK-dependent pathway leads to cytoskeleton disruption in Ras-transformed fibroblasts.
TLDR
The Ras/MAPK pathway is established as the critical pathway involved in cytoskeleton disruption during Ras-transformation, and a new mechanism, involving alteration in ROCKI/Rho-kinase expression, is suggested by which oncogenic Ras can specifically target the actin-based cytos skeleton and achieve morphological transformation of the cells.
Induction of β3-Integrin Gene Expression by Sustained Activation of the Ras-Regulated Raf–MEK–Extracellular Signal-Regulated Kinase Signaling Pathway
TLDR
It is demonstrated that the Ras-activated Raf–MEK–extracellular signal-regulated kinase (ERK) signaling pathway can specifically control the expression of individual integrin subunits in a variety of human and mouse cell lines, and oncogene-induced alterations in integrin gene expression may participate in the changes in cell adhesion and migration that accompany the process of oncogenic transformation.
Serine and threonine phosphorylation of the paxillin LIM domains regulates paxillin focal adhesion localization and cell adhesion to fibronectin.
TLDR
The first demonstration of the regulation of protein localization through LIM domain phosphorylation is demonstrated and a novel mechanism of regulating LIM domain function is suggested that contributes to "inside-out" integrin-mediated signal transduction.
Paxillin null embryonic stem cells are impaired in cell spreading and tyrosine phosphorylation of focal adhesion kinase
TLDR
It is demonstrated that paxillin contributes to attachment-dependent tyrosine phosphorylation of FAK and early cell spreading in ES cells.
Phosphorylation of Paxillin via the ERK Mitogen-activated Protein Kinase Cascade in EL4 Thymoma Cells*
TLDR
A novel inside-out signaling pathway by which the ERK cascade may regulate events involved in adhesion is described by which Paxillin was phosphorylated on serine/threonine residues in response to PMA treatment.
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