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Pathway Description
Fc Epsilon Receptor I Signaling in Mast Cells
Bos taurus
Category:
Protein Pathway
Sub-Categories:
Immunological
Cytokine Signaling
Kinase Signaling
Cellular Response
Created: 2018-08-31
Last Updated: 2019-09-12
Fc epsilon receptor 1 (Fc epsilon RI) is a high-affinity receptor for the Fc region of immunoglobulin E (IgE), an antibody isotope involved in allergies. The antigens of allergens bind to IgE antibodies, which then interact with Fc epsilon RIs on the surface of mast cells. This activates the mast cells and results in degranulation, a process by which preformed granules containing histamine, proteoglycans, and serine proteases, are released. Activated mast cells also synthesize and secrete lipid-derived mediators (such as prostaglandins, leukotrienes, and platelet-activating factor) and cytokines (notably tumor necrosis factor-alpha, interleukin-4, and interleukin-5). The release of these compounds results in the inflammatory response.
References
Fc Epsilon Receptor I Signaling in Mast Cells References
Collins RA, Gelder KI, Howard CJ: Nucleotide sequence of cattle FcGRIII: its identification in gammadelta T cells. Immunogenetics. 1997;45(6):440-3.
Pubmed: 9089104
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
Morton HC, Storset AK, Brandtzaeg P: Cloning and sequencing of a cDNA encoding the bovine FcR gamma chain. Vet Immunol Immunopathol. 2001 Sep 28;82(1-2):101-6.
Pubmed: 11557297
Edwards JC, Kapadia S: Regulation of the bovine kidney microsomal chloride channel p64 by p59fyn, a Src family tyrosine kinase. J Biol Chem. 2000 Oct 13;275(41):31826-32. doi: 10.1074/jbc.M005275200.
Pubmed: 10930415
Yang W, Cerione RA: Cloning and characterization of a novel Cdc42-associated tyrosine kinase, ACK-2, from bovine brain. J Biol Chem. 1997 Oct 3;272(40):24819-24. doi: 10.1074/jbc.272.40.24819.
Pubmed: 9312079
Lin Q, Lo CG, Cerione RA, Yang W: The Cdc42 target ACK2 interacts with sorting nexin 9 (SH3PX1) to regulate epidermal growth factor receptor degradation. J Biol Chem. 2002 Mar 22;277(12):10134-8. doi: 10.1074/jbc.M110329200. Epub 2002 Jan 17.
Pubmed: 11799118
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
Otsu M, Hiles I, Gout I, Fry MJ, Ruiz-Larrea F, Panayotou G, Thompson A, Dhand R, Hsuan J, Totty N, et al.: Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase. Cell. 1991 Apr 5;65(1):91-104. doi: 10.1016/0092-8674(91)90411-q.
Pubmed: 1707345
Panayotou G, Bax B, Gout I, Federwisch M, Wroblowski B, Dhand R, Fry MJ, Blundell TL, Wollmer A, Waterfield MD: Interaction of the p85 subunit of PI 3-kinase and its N-terminal SH2 domain with a PDGF receptor phosphorylation site: structural features and analysis of conformational changes. EMBO J. 1992 Dec;11(12):4261-72.
Pubmed: 1330535
Kazlauskas A, Kashishian A, Cooper JA, Valius M: GTPase-activating protein and phosphatidylinositol 3-kinase bind to distinct regions of the platelet-derived growth factor receptor beta subunit. Mol Cell Biol. 1992 Jun;12(6):2534-44. doi: 10.1128/mcb.12.6.2534.
Pubmed: 1375321
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
Davis AR, Clements MK, Bunger PL, Siemsen DW, Quinn MT: Cloning and characterization of bovine low molecular weight GTPases (Rac1 and Rac2) and rho GDP-dissociation inhibitor 2 (D4-GDI). Vet Immunol Immunopathol. 2000 May 23;74(3-4):285-301.
Pubmed: 10802295
Kobayashi K, Kuroda S, Fukata M, Nakamura T, Nagase T, Nomura N, Matsuura Y, Yoshida-Kubomura N, Iwamatsu A, Kaibuchi K: p140Sra-1 (specifically Rac1-associated protein) is a novel specific target for Rac1 small GTPase. J Biol Chem. 1998 Jan 2;273(1):291-5. doi: 10.1074/jbc.273.1.291.
Pubmed: 9417078
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
Harhay GP, Sonstegard TS, Keele JW, Heaton MP, Clawson ML, Snelling WM, Wiedmann RT, Van Tassell CP, Smith TP: Characterization of 954 bovine full-CDS cDNA sequences. BMC Genomics. 2005 Nov 23;6:166. doi: 10.1186/1471-2164-6-166.
Pubmed: 16305752
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 SMP0000358
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