As of phosphotyrosine antique Body, found in the specific area of the substrate EVENT EGF stimulation Promoted CAS SD phosphorylation, YM155 which was blocked by inhibiting Src measured detect. In the absence of stimulation by a growth factor, cells, which constitutively active enlarged SRCA FG Ert CAS SD phosphorylation abolished by inhibiting Src. These results demonstrate that Src activity t For phosphorylation of CAS SD in FG pancreatic cancer cells is necessary. Previous studies have shown that a completely’s Full range of SD protein assembly Liegepl protect EVENT leads to loss of cell migration on various matrix proteins inhibit. However, little is known about the specificity of these phosphorylation events is known and especially when regulate cell invasion mediated by EGF or metastases.
There are 15 subjects that CAS SD tyrosine phosphorylation represent putative Src. To determine whether these sites are sensitive to Src activity Were t, we pressed NVP-AUY922 fa Steady WT CAS or CAS, the mutations YF-15 phosphorylation in cells YXXP SD FG. EGF stimulation leads to phosphorylation by Src h Depends WT CAS, w While cells containing mutated the F1 15 CAS showed no phosphorylation. In order to evaluate r EGF-induced phosphorylation of the SD EVENT migration, cells or the WT FG F1 allowed 15 CAS designs migrate to vitronectin or fibronectin in the presence or absence of EGF. On vitronectin, WT CAS FG EGF expression in response to stimulation of a Similar manner to non-transfected cells or vector control cells FG FG.
In cells, the 15 F1, has not EGF induced a response mediated migration on vitronectin v5, although the migration on fibronectin was normal, suggesting that one or more locations within the CAS SD are seriously involved in migration v5 GEF mediation h depends. To better identify the region within the SD, the v5 for inducible GEF migration, we expressed fa Continuously on two SD mutants in these cells. Expression of EGF blocked F1 9 induced migration on vitronectin, indicating that tyrosine phosphorylation first September for the EGF-dependent-Dependent Src-mediated migration v5 response is required. It is important that the expression of these cell mutations CAS FG not significantly affect cell migration mediated by collagen or fibronectin. These results suggest that play one or more of the nine tyrosines in the substrate CAS an r Specifically in the migration induced v5.
CAS phosphorylation is commonly associated with the frontal and actin cytoskeleton organization lacing membrane processes, which are essential in cell invasion. FG cells caused EGF stimulation actin reorganization of stress fibers in filopodia, and this was blocked by inhibition of Src. We observed anything similar pattern in cells F10 15, w While cells which showed little or no F1 9 EGF-induced actin reorganization. To determine an r Regulated by small GTPases of the CAS in actin cytoskeleton organization, we examined the state of activation of four small GTPases in cell F1 or F10 FG 15 9 mutations. EGF stimulation activates Rac1 and Rho in vector control cells FG, F10 or F1 15 9 mutations. In contrast, the EGF-dependent-Dependent activation of Rap1 is a positive regulat