growth and metastasis. PLCγ1 is acting as a vital part in stopping apoptosis in cells, and thus by inhibiting PLCγ1 the body better allows programmed cell death and avoidance of tumors. The main role found for PLCγ1 is cell growth, and this role in specific is why it is becoming more commonly studied for anti-cancer drugs. Tissue samples from cancer patients the PLCγ1 levels are not elevated, however, regulatory factors for this proteins are lowered and that amplification of PLCγ1 is extremely high. The regulatory proteins that stop PLCγ1 have been turned off by the cell, which means that while there is no increase in the physical protein PLCγ1 there is an increase in how much work it is doing - nothing is stopping it from over working itself. Studies also showed that adding new regulatory to cells in vitro helped reduce previously amplified PLCγ1. This information has encouraged PLCγ1 becoming an anti-cancer drug target despite the issues that come with targeting intermembrane proteins. Interactions PLCG1 has been shown to interact with: BAG3, CD117, CD31, Cbl gene CISH Epidermal growth factor receptor, Eukaryotic translation elongation factor 1 alpha 1, FLT1, GAB1, GIT1, Grb2, HER2/neu, IRS2, ITK, KHDRBS1, Linker of activated T cells, Lymphocyte cytosolic protein 2, PDGFRA, PLD2, RHOA, SOS1, TUB, TrkA, TrkB, VAV1, and Wiskott-Aldrich syndrome protein. See also Phospholipase C References Peripheral membrane proteins EC 3.1.4