Publications by authors named "Fatima Burovic"
Article Synopsis
- PDGF-BB binds to its receptors, activating several signaling pathways crucial for cell survival and growth, particularly in mesenchymal cells.
- Erk5 MAP kinase activation in smooth muscle cells is regulated by various proteins including Mekk2, Mek1/2, and PKC, illustrating the interplay between Erk1/2 and Erk5 pathways.
- Although Erk5 does not accumulate in the nucleus upon PDGF-BB stimulation, it is essential for Smad1/5/8 signaling, which is mediated through bone morphogenetic proteins (BMPs), indicating its role in gene expression regulation in the cytoplasm.
Extracellular regulated kinase (Erk) 5 is a member of the mitogen activated protein (MAP) kinase family that has been implicated in both cell proliferation and survival. In the present study, we found that stimulation with platelet-derived growth factor (PDGF)-BB leads to a transient activation of Erk5, which was shown to be dependent on recruitment of both Src kinases and the tyrosine phosphatase Shp2 to the activated PDGF receptor beta (PDGFRbeta). We could also demonstrate that Shp2 docking to the receptor is critical for Src kinase activation, suggesting that Shp2 may contribute to Erk5 activation through its involvement in Src kinase activation.
View Article and Find Full Text PDFIncreased glycolysis is characteristic of malignancy. Previously, with a mitochondrial inhibitor, we demonstrated that glycolytic ATP production was sufficient to support migration of melanoma cells. Recently, we found that glycolytic enzymes were abundant and some were increased in pseudopodia formed by U87 glioma (astrocytoma) cells.
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