For example, when activated, fibroblast growth factor receptor 1 and epidermal growth factor receptor are RTKs that have phosphorylated tyrosines, which provide docking sites for PLCG1 SH2 domains. The activated RTKs phosphoylate PLCG1 at tyrosines located at position 472, 771, 775, 783, and 1254. Non-receptor tyrosine kinases interact with PLCG1 in large complexes at the plasma membrane. For example, in T cells, Lck and Fyn (Src family kinases) phosphorylate immunoreceptor tyrosine-based activation motifs (ITAMs) on the T-cell antigen receptor (TCR). The phosphorylated ITAMs recruit ZAP-70, which phosphorylates tyrosines in LAT and SLP-76. PLCg1 binds to LAT through its n-terminal SH2 domain and to SLP-76 via its SH3 domain. Has been shown to interact with CISH which negatively regulates it by targeting it for degradation. The deletion of Cish in effector T cells has been shown to augment TCR signaling and subsequent effector cytokine release, proliferation and survival. The adoptive transfer of tumor-specific effector T cells knocked out or knocked down for CISH resulted in a significant increase in functional avidity and long-term tumor immunity. There are no changes in activity or phosphorylation of Cish's purported target, STAT5 in either the presence or absence of Cish. In vitro studies have shown signs of PLCγ1 having many cell-motility functions, however in vivo have not been able to show a physiological role for PLCγ1. While PLCγ1 is well documented and easily found in the body, clear connections and roles for PLCγ1 have been difficult to find in in vivo studies. Despite this, there is still able to find links between levels of PLCγ1 and cancer patient survivability. Cancer While there is a strong link between PLCγ1 and tumor growth/cancer progression, most research is in early stages. Cancer is also a very unique illness in that every patient has different needs. Information here is not to be used as treatment and instead as a way to better understand cancer progression.Mutations in PLCγ1 can lead to cancer cell proliferations and inhibition can lead to tumor growth. PLCγ1 is involved in cell proliferation, and mutations cause it to be over expressed and help the progression of tumor cells. This aspect of PLCγ1 also helps cancer migration and metastasis away from the original tumor cells. There is also a link between PLCγ1 and PDK, the PDK-PLCγ1 pathway, which is a vital part of cancer cell invasion. The inhibition of PLCγ1 is linked to a decrease in tumor