Talk:PLCG1

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The current article lacks general information about the domains specific to the PLCg1 isozyme and how it is activated in signaling pathways. My addition to the current article is as follows:

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 have phosphorylated tyrosines, which provide docking sites for PLCg1 SH2 domains^[2]. The activated RTKs phosphoylate PLCg1 at tyrosines located at position 472, 771, 775, 783, and 1254^[3]. 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^[2].

I will be adding my edits under the function tab or under the lead section. Suggestions of where to add my info?Lbates2008 (talk) 15:29, 13 March 2017 (UTC)[reply]

References

^ Singh, Shaneen M.; Murray, Diana (2003). "Molecular modeling of the membrane targeting of phospholipase C pleckstrin homology domains". Protein Science. 12: 1934-1953.
^ ^a ^b ^c Gresset, Aurelie; Sondek, John; Harden, T. Kendall (2012). "The Phospholipase C Isozymes and Their Regulation". Subcell Biochem. 58: 61-94.
^ Bae, JH; Lew, ED; Yuzawa, S; Tomé, F; Lax, I; Schlessinger, J (7 August 2009). "The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site". Cell. 138 (3): 514–24. PMID 19665973.

Wiki Education Foundation-supported course assignment

This article is or was the subject of a Wiki Education Foundation-supported course assignment. Further details are available on the course page. Student editor(s): Lbates2008. Peer reviewers: KP 0503, Ncameron2013.

Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT (talk) 10:43, 18 January 2022 (UTC)[reply]

Wiki Education Foundation-supported course assignment

This article was the subject of a Wiki Education Foundation-supported course assignment, between 1 September 2020 and 17 December 2020. Further details are available on the course page. Student editor(s): DKitch21. Peer reviewers: Wickypears, KC1200.

Above undated message substituted from Template:Dashboard.wikiedu.org assignment by PrimeBOT (talk) 10:43, 18 January 2022 (UTC)[reply]

[Singh-1] Singh, Shaneen M.; Murray, Diana (2003). "Molecular modeling of the membrane targeting of phospholipase C pleckstrin homology domains". Protein Science. 12: 1934-1953.

[Gresset-2] Gresset, Aurelie; Sondek, John; Harden, T. Kendall (2012). "The Phospholipase C Isozymes and Their Regulation". Subcell Biochem. 58: 61-94.

[Bae-3] Bae, JH; Lew, ED; Yuzawa, S; Tomé, F; Lax, I; Schlessinger, J (7 August 2009). "The selectivity of receptor tyrosine kinase signaling is controlled by a secondary SH2 domain binding site". Cell. 138 (3): 514–24. PMID 19665973.

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