A number of the overlapping proteins (ERK1, ERK2, IRS2, GAB1, SHB, SHC and PI3K p85-alpha) are key signaling intermediates for multiple signaling pathways.
In fact, only the phosphorylation signals of Eps8, PLC-γ1 (at Y783), and Shc (at Y239/240) showed no change under these variables (Fig. 2).
The Src-induced phosphorylation of Eps8, PLC-γ1 and Shc (poY239/poY240) were not affected by either FAK or adherence status.
PTP-PEST associates with the adaptor proteins Grb2 [60] and Shc [62], [63], both of which participate in the growth factor signaling and motility.
Upon insulin stimulation, IR is activated through autophosphorylation, and consequently phosphorylates several insulin receptor substrate (IRS) proteins, including IRS1-6, Shc and Gab1.
Activation of Met by HGF leads to receptor dimerization and recruitment of adaptor (GAB1, Grb2, Shc) and signaling (Ras/MAPK, PI3K/Akt, Src, STAT, Shp2) proteins.
Fig. 2 SHC versus temperature for molten salt and nanofluids with different GNP concentrations for temperature range from 150 to 450 °C.
This apparent pattern conversion was not observed in the upstream positive effectors of ERK1, such as EGFR, Grb2, Shc, Shp2, and Plcγ1.
Some proteins, such as Grb2 [45], [45], Shc [45], [46], Grb7 and Crk [47] interact with APP only when Tyr682 is phosphorylated; others, like Fe65, Fe65L1 and Fe65L2 only when this tyrosine is not phosphorylated [48].
