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Pathway Description
Activation of PKC Through G Protein-Coupled Receptor
Bos taurus
Category:
Metabolite Pathway
Sub-Category:
Signaling
Created: 2018-08-31
Last Updated: 2019-08-16
G protein-coupled receptors sense stimuli outside the cell and transmit signals across the plasma membrane. Activation of protein kinase C (PKC) is one of the common signaling pathways. When a class of GPCRs are activated by a ligand, they activate Gq protein to bind GTP instead of GDP. After the Gq becomes active, it activates phospholipase C (PLC) to cleave the membrane lipid phosphatidylinositol 4,5-bisphosphate (PIP2) into inositol 1,4,5-trisphosphate (IP3) and diacyl glycerol (DAG). IP3 can bind Ins3P receptor to open calcium channel by diffusion from cytoplasm to ER. Activated calcium channel will release the calcium from ER into cytoplasm. Calcium can activate the kinase activity of PKC.
References
Activation of PKC Through G Protein-Coupled Receptor References
Yoo SH, Oh YS, Kang MK, Huh YH, So SH, Park HS, Park HY: Localization of three types of the inositol 1,4,5-trisphosphate receptor/Ca(2+) channel in the secretory granules and coupling with the Ca(2+) storage proteins chromogranins A and B. J Biol Chem. 2001 Dec 7;276(49):45806-12. doi: 10.1074/jbc.M107532200. Epub 2001 Oct 2.
Pubmed: 11584008
Marks AR, Tempst P, Chadwick CC, Riviere L, Fleischer S, Nadal-Ginard B: Smooth muscle and brain inositol 1,4,5-trisphosphate receptors are structurally and functionally similar. J Biol Chem. 1990 Dec 5;265(34):20719-22.
Pubmed: 2174422
Schlossmann J, Ammendola A, Ashman K, Zong X, Huber A, Neubauer G, Wang GX, Allescher HD, Korth M, Wilm M, Hofmann F, Ruth P: Regulation of intracellular calcium by a signalling complex of IRAG, IP3 receptor and cGMP kinase Ibeta. Nature. 2000 Mar 9;404(6774):197-201. doi: 10.1038/35004606.
Pubmed: 10724174
Nakamura F, Ogata K, Shiozaki K, Kameyama K, Ohara K, Haga T, Nukada T: Identification of two novel GTP-binding protein alpha-subunits that lack apparent ADP-ribosylation sites for pertussis toxin. J Biol Chem. 1991 Jul 5;266(19):12676-81.
Pubmed: 1905731
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
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 SMP0000749
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