Pervanadate-induced reverse translocation and tyrosine phosphorylation of phorbol ester-stimulated protein kinase C βII are mediated by Src-family tyrosine kinases in porcine neutrophils

Takahashi, Hideyuki; Suzuki, Kingo; Namiki, Hideo

doi:10.1016/j.bbrc.2003.12.163

Cited by 14 publications

(11 citation statements)

References 46 publications

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“…In order to verify that Src activation was detected by SrcI, U87 cells were treated with pervanadate, a phosphatase inhibitor. Indeed, treatment with phosphatase inhibitors is known to increase both Src and FAK phosphorylation [1,[40][41][42], but also to induce peripheral adhesion rearrangement [1,43,44]. In our cells, addition of pervanadate induces Src activation as visualized in Western blots by the increase in P-SrcY418 levels both in non transfected and in SrcI-transfected U87 cells compared to non treated cells (Fig.…”

Section: Resultsmentioning

confidence: 71%

Src activation and translocation from focal adhesions to membrane ruffles contribute to formation of new adhesion sites

Hamadi

Deramaudt

Takeda

et al. 2008

Cell. Mol. Life Sci.

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Cell migration requires the coordinated turnover of focal adhesions, a process that involves FAK phosphorylation. Since Src is the major kinase implicated in FAK phosphorylation, we focus here on the role of Src activation on adhesion remodelling. In astrocytoma cells, constitutively activated Src induces both FAK phosphorylation and adhesion rearrangement. To evaluate how Src controls these processes, we used a recently described Src reporter to monitor the dynamics of Src phosphorylation. Upon Src activation, focal adhesions started to disassemble while Src appeared highly expressed at newly formed membrane ruffles. Kinetic analysis of time-lapse movies showed that loss of phospho-Src at focal adhesions was time-correlated with the appearance of membrane ruffles containing phospho-Src. Moreover, FLIP analysis revealed a dynamic equilibrium of Src between focal adhesions and membrane ruffles. We conclude that upon phosphorylation, Src is directly translocated from focal adhesions to membrane ruffles, thereby promoting formation of new adhesion complexes.

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Section: Resultsmentioning

confidence: 71%

Src activation and translocation from focal adhesions to membrane ruffles contribute to formation of new adhesion sites

Hamadi

Deramaudt

Takeda

et al. 2008

Cell. Mol. Life Sci.

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“…The reactive oxygen species have also been shown to enhance the Src activity (Boulven et al, 2002; Huyer et al, 1997; Takahashi et al, 2004). This combined effect of phosphatase inhibition and Src kinase activation by ROS can highlight Src phosphorylation efficiency on the biosensors to cause their FRET change.…”

Section: Resultsmentioning

confidence: 99%

Visualization of Src Activity at Different Compartments of the Plasma Membrane by FRET Imaging

Seong

Ouyang

et al. 2009

Chemistry & Biology

100

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Summary Membrane compartments function as segregated signaling platforms for different cellular functions. It is not clear how Src is regulated at different membrane compartments. To visualize local Src activity in live cells, a FRET-based Src biosensor was targeted in or outside of lipid rafts at the plasma membrane, via acylation or prenylation modifications on targeting tags either directly fused to the biosensor or coupled to the biosensor through an inducible heterodimerization system. In response to growth factors and pervanadate, the induction of Src activity in rafts was slower and weaker, dependent on actin and possibly its mediated transportation of Src from perinuclear regions to the plasma membrane. In contrast, the induction of Src activity in non-rafts was faster and stronger, dependent on microtubules. Hence, the Src activity is differentially regulated via cytoskeleton at different membrane compartments.

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“…Many data points at close interaction between c-Src and members of the PKC superfamily (Longo et al 2004, Takahashi et al 2004, and much consistent evidence indicates an important role for c-Src in osteoblast differentiation (Marzìa et al 2000). In view of these data, we explored the possibility of a c-Src role on F-promoter regulation.…”

Section: Discussionmentioning

confidence: 99%

Modulation of human estrogen receptor α F promoter by a protein kinase C/c-Src-dependent mechanism in osteoblast-like cells

Longo¹,

Peruzzi²,

Fortunati³

et al. 2006

Journal of Molecular Endocrinology

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The human estrogen receptor a (ERa) gene is driven by multiple promoters, of which the F promoter alone is found to be active in primary osteoblasts. The study was aimed at identifying new regulatory pathways affecting transcription of the receptor in this cell lineage. We generated human osteoblast-like cells, Saos-2, stably transfected with a luciferase-reporter gene downstream of the human ERa F promoter (Saos F-Luc), and assayed the reporter response to differentiation-related signals. Over-confluence, shown to stimulate osteoblast differentiation, caused a time-dependent increase of F-promoter activity and correlated with an inactivation of protein kinase C a (PKCa). PKC downregulation, obtained by long-term treatment with phorbol 12-myristate 13-acetate (PMA), resulted in promoter stimulation at similar levels in sub-confluent cells. The F promoter contains a putative PMA-responsive AP-1 site, but AP-1 activation was unremarkable in overconfluent cells. Treatment with PP1, a specific inhibitor of the non-receptor tyrosine-kinase c-Src, which is a negative regulator of osteoblast differentiation, showed that the activity of this kinase inhibits the F promoter. In PP1-treated cells, Fpromoter activity was not further increased by PMA. Treatment with the generic kinase inhibitor 4-dimethylaminopyridine (DMAP) resulted in a dose-dependent induction of the promoter, which matched a parallel decrease of active c-Src. The effect was c-Src dependent, as DMAP caused no further promoter induction in PP1-treated cells. Overexpression of exogenous human ERa resulted in modest promoter stimulation, which required the ligand-independent activator function 1 of the receptor. In murine primary osteoblasts, additional ERa signal was observed upon induction of F promoter. In conclusion, we demonstrated a robust PKC/c-Src-dependent and estrogen-independent mechanism modulating transcription of ERa in osteoblasts, probably affecting estrogen responsiveness during cell differentiation.

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Pervanadate-induced reverse translocation and tyrosine phosphorylation of phorbol ester-stimulated protein kinase C βII are mediated by Src-family tyrosine kinases in porcine neutrophils

Cited by 14 publications

References 46 publications

Src activation and translocation from focal adhesions to membrane ruffles contribute to formation of new adhesion sites

Src activation and translocation from focal adhesions to membrane ruffles contribute to formation of new adhesion sites

Visualization of Src Activity at Different Compartments of the Plasma Membrane by FRET Imaging

Modulation of human estrogen receptor α F promoter by a protein kinase C/c-Src-dependent mechanism in osteoblast-like cells

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