Their results showed that TCR-induced PI3K/Akt activation needs both membrane translocation and tyrosine phosphorylation of SLP-76 as well as LAT for the localization of SLP-76 to the membrane. A critical role for both LAT and SLP-76 has been demonstrated through reconstitution of LAT-deficient Jurkat T cell lines with LAT or SLP-76 deliberately targeted to the rafts. We have found lower AbMole Aristolochic-acid-A c-value for SLP-76 in an unperturbed TCR signaling AbMole Diperodon pathway. In contrast, it has became 0.60307 and 0.5495 in pathogen perturbed system and in the system, where it is optimized for two conflicting objective functions, respectively. In the same manner, we have found lower c-value for LAT in an unperturbed TCR signaling pathway. In contrast, it has become 0.57508 and 0.15188 in pathogen perturbed system and in the system, where it is optimized for two conflicting objective functions, respectively. In LAT-deficient J.Cam2 and ANJ3 cells, PLCc1, VAV and SLP76 phosphorylation were not detected and TCR-mediated signaling events were found to be impaired. Early T cell development has been found to be blocked in LAT-negative mice similar to that observed in mice, in which either LCK and FYN, or ZAP70 and Syk was deleted. These observations demonstrate that LAT is an obligatory step, downstream of LCK and ZAP70, and is an important link to Ras/ MAP kinase and PLCc1 pathways. Dlg1 is expressed in all T cell developmental stages and forms a stable complex with LCK. It functions as a negative regulator of T cell activation. Endogenous Dlg1 connects with TCRf and CBL. The transient overexpression of Dlg1 attenuates basal and VAV1-induced NFAT reporter activation. It is also shown that the reduction of Dlg1 expression by RNA interference enhances both CD3- and SAg-mediated NFAT activation. Thus it is interpreted that Dlg1 acts as an activation antagonist. This is the reason, we have got higher c-value for Dlgh1 in an unperturbed TCR signaling pathway. In contrast, it has become 0 and 0.46094 in pathogen perturbed system and in the system, where it is optimized for two conflicting objective functions, respectively. The cytoskeleton of eukaryotic cells has a pivotal role in hostpathogen interactions as it is essential for epithelial and endothelial barrier functions. It limits the invasion and dissemination of pathogens in tissues. GTP-binding proteins of the Rho family are regulators of the actin cytoskeleton, and Rho proteins play essential roles in host cell invasion by bacteria. They are the targets for bacterial protein toxins that either inactivate GTPases by ADP-ribosylation or glucosylation, or activate them by deamidation. Specifically, Rho GTPase Cdc42 regulates cytoskeletal changes at the immunological synapse that are critical to T cell activation.