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Pathway Description
Phospholipase C Signaling Pathway
Bos taurus
Category:
Protein Pathway
Sub-Categories:
Gene Regulatory
Kinase Signaling
Cellular Response
Created: 2018-08-31
Last Updated: 2019-09-13
Phospholipase C pathways is one of the major intracellular signalling pathways regulating hormones. It functions to activate inositol lipid signalling pathways causing the hydrolysis of PIP2 by PLC to IP3 and diacylglycerol to activate protein kinase C. IP3 releases calcium from the endoplasmic reticulum. PIP3 is an important regulator of AKT signaling and downstream pathways.
References
Phospholipase C Signaling Pathway References
Katan M, Kriz RW, Totty N, Philp R, Meldrum E, Aldape RA, Knopf JL, Parker PJ: Determination of the primary structure of PLC-154 demonstrates diversity of phosphoinositide-specific phospholipase C activities. Cell. 1988 Jul 15;54(2):171-7. doi: 10.1016/0092-8674(88)90549-1.
Pubmed: 2455601
Ryu SH, Kim UH, Wahl MI, Brown AB, Carpenter G, Huang KP, Rhee SG: Feedback regulation of phospholipase C-beta by protein kinase C. J Biol Chem. 1990 Oct 15;265(29):17941-5.
Pubmed: 2211670
Stahl ML, Ferenz CR, Kelleher KL, Kriz RW, Knopf JL: Sequence similarity of phospholipase C with the non-catalytic region of src. Nature. 1988 Mar 17;332(6161):269-72. doi: 10.1038/332269a0.
Pubmed: 2831461
Kim JW, Sim SS, Kim UH, Nishibe S, Wahl MI, Carpenter G, Rhee SG: Tyrosine residues in bovine phospholipase C-gamma phosphorylated by the epidermal growth factor receptor in vitro. J Biol Chem. 1990 Mar 5;265(7):3940-3.
Pubmed: 1689310
Wahl MI, Nishibe S, Kim JW, Kim H, Rhee SG, Carpenter G: Identification of two epidermal growth factor-sensitive tyrosine phosphorylation sites of phospholipase C-gamma in intact HSC-1 cells. J Biol Chem. 1990 Mar 5;265(7):3944-8.
Pubmed: 1689311
Zimin AV, Delcher AL, Florea L, Kelley DR, Schatz MC, Puiu D, Hanrahan F, Pertea G, Van Tassell CP, Sonstegard TS, Marcais G, Roberts M, Subramanian P, Yorke JA, Salzberg SL: A whole-genome assembly of the domestic cow, Bos taurus. Genome Biol. 2009;10(4):R42. doi: 10.1186/gb-2009-10-4-r42. Epub 2009 Apr 24.
Pubmed: 19393038
Coffer PJ, Woodgett JR: Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families. Eur J Biochem. 1991 Oct 15;201(2):475-81. doi: 10.1111/j.1432-1033.1991.tb16305.x.
Pubmed: 1718748
Coffer PJ, Woodgett JR: Molecular cloning and characterisation of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families. Eur J Biochem. 1992 May 1;205(3):1217.
Pubmed: 1533586
Gao T, Furnari F, Newton AC: PHLPP: a phosphatase that directly dephosphorylates Akt, promotes apoptosis, and suppresses tumor growth. Mol Cell. 2005 Apr 1;18(1):13-24. doi: 10.1016/j.molcel.2005.03.008.
Pubmed: 15808505
Parker PJ, Coussens L, Totty N, Rhee L, Young S, Chen E, Stabel S, Waterfield MD, Ullrich A: The complete primary structure of protein kinase C--the major phorbol ester receptor. Science. 1986 Aug 22;233(4766):853-9. doi: 10.1126/science.3755547.
Pubmed: 3755547
Nishizuka Y: The molecular heterogeneity of protein kinase C and its implications for cellular regulation. Nature. 1988 Aug 25;334(6184):661-5. doi: 10.1038/334661a0.
Pubmed: 3045562
Cazaubon SM, Parker PJ: Identification of the phosphorylated region responsible for the permissive activation of protein kinase C. J Biol Chem. 1993 Aug 15;268(23):17559-63.
Pubmed: 8349635
This pathway was propagated using PathWhiz -
Pon, A. et al. Pathways with PathWhiz (2015) Nucleic Acids Res. 43(Web Server issue): W552–W559.
Propagated from SMP0063783
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