PLCγ1 is a cell growth factor from the
PLC superfamily. PLCγ1 is used during cell growth and apoptosis, It is part of the
PIP3 pathway and leads to and increase in calcium in the cells. In
neuronal cells, PLCγ1 is highly involved in actin
cytoskeleton organization and
synaptic plasticity. Two transcript variants encoding different isoforms have been found for this gene. Common to all PLC isozymes, PLCG1 consists of an N-terminal PH domain, which translocates PLC to the plasma membrane and binds PIP3; four EF hands; an X and Y catalytic region comprising the TIM barrel; and a C-terminal C2 domain. Specific to the PLCG isozymes is a large separation between the X and Y domains consisting of a split PH domain, tandem SH2 domains, and an SH3 domain. 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 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 ==