I am adding onto the existing article on PLCg1. I think I'm going to add my paragraphs under the function tab:

Common to all PLC isozymes, PLCg1 consists of an N-terminal PH ___domain, which translocates PLC to the plasma membrane and binds PIP3 ([1]), 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. The SH2 domains bind phosphorylated tyrosine residues on target proteins via their FLVR sequence motifs, activating the catalytic function of PLCg; and the SH3 ___domain binds to proline-rich sequences on the target protein ([2]).

PLCg1 can be activated by receptor tyrosine kinases (RTKs) and non-receptor tyrosine kinases. For example, when activated, fibroblast growth factor receptor 1 and epidermal growth factor receptor are RTKs that, upon ligand binding, have phosphorylated tyrosine residues, which provide docking sites for PLCg1 SH2 domains ([3]). The activated RTKs phosphorylate PLCg1 at tyrosines located at position 472, 771, 775, 783, and 1254[4]. 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 ([3]).

  1. ^ Singh, Shaneen M.; Murray, Diana. "Molecular modeling of the membrane targeting of phospholipase C pleckstrin homology domains". Protein Science. 12 (9): 1934–1953. doi:10.1110/ps.0358803. PMC 2323991. PMID 12930993.{{cite journal}}: CS1 maint: PMC format (link)
  2. ^ Gresset, Aurelie; Hicks, Stephanie N.; Harden, T. Kendall; Sondek, John (2010-11-12). "Mechanism of Phosphorylation-induced Activation of Phospholipase C-γ Isozymes". Journal of Biological Chemistry. 285 (46): 35836–35847. doi:10.1074/jbc.M110.166512. ISSN 0021-9258. PMC 2975207. PMID 20807769.{{cite journal}}: CS1 maint: PMC format (link) CS1 maint: unflagged free DOI (link)
  3. ^ a b Gresset, Aurelie; Sondek, John; Harden, T. Kendall (2012-01-01). Balla, Tamas; Wymann, Matthias; York, John D. (eds.). Phosphoinositides I: Enzymes of Synthesis and Degradation. Subcellular Biochemistry. Springer Netherlands. pp. 61–94. doi:10.1007/978-94-007-3012-0_3. ISBN 9789400730113. PMC 3638883. PMID 22403074.{{cite book}}: CS1 maint: PMC format (link)
  4. ^ Bae, Jae Hyun; Lew, Erin Denise; Yuzawa, Satoru; Tomé, Francisco; Lax, Irit; Schlessinger, Joseph. "The Selectivity of Receptor Tyrosine Kinase Signaling Is Controlled by a Secondary SH2 Domain Binding Site". Cell. 138 (3): 514–524. doi:10.1016/j.cell.2009.05.028. PMC 4764080. PMID 19665973.{{cite journal}}: CS1 maint: PMC format (link)