Loading Pathway...
Error: Pathway image not found.
Hide
Pathway Description
Ion Channel and Phorbal Esters Signaling Pathway
Bos taurus
Category:
Protein Pathway
Sub-Categories:
Kinase Signaling
Cellular Response
Created: 2018-09-20
Last Updated: 2019-08-16
Molecules transmitting signals into cells often act through receptors in the plasma membrane that stimulate production of second messengers. When activated by a plasma membrane receptor, the enzyme phospholipase C (PLCg) hydrolyzes the membrane lipid phosphatidylinositol (PIP2) into the second messengers diacylglycerol (DAG) and IP3. IP3 releases calcium from intracellular stores into the cytoplasm where calcium alters many cellular activities, including activating protein kinase C. DAG also activates protein kinase C. Biologists often study signaling by artificially manipulating pathways using molecules like ionomycin and phorbol esters as research tools. Ionomycin is a molecule that carries calcium through the plasma membrane to increase the calcium concentration in the cytoplasm and activate protein kinase C without activating phospholipase C. Phorbol esters are molecules that mimic the action of DAG in the activation of protein kinase C, and were originally identified as tumor-promoting agents. The combination of ionomycin and phorbol esters is often used experimentally to study the effect of calcium and DAG signaling in cellular responses like T cell activation.
References
Ion Channel and Phorbal Esters Signaling Pathway References
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
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
Coussens L, Parker PJ, Rhee L, Yang-Feng TL, Chen E, Waterfield MD, Francke U, Ullrich A: Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signaling pathways. Science. 1986 Aug 22;233(4766):859-66. doi: 10.1126/science.3755548.
Pubmed: 3755548
Sneyers M, Kettmann R, Massart S, Renaville R, Burny A, Portetelle D: Cloning and characterization of a cDNA encoding the beta-subunit of the bovine insulin-like growth factor-1 receptor. DNA Seq. 1991;1(6):405-6.
Pubmed: 1662995
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 SMP0090032
Highlighted elements will appear in red.
Highlight Compounds
Highlight Proteins
Enter relative concentration values (without units). Elements will be highlighted in a color gradient where red = lowest concentration and green = highest concentration. For the best results, view the pathway in Black and White.
Visualize Compound Data
Visualize Protein Data
Downloads
Settings