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Pathway Description
Insulin Signalling
Bos taurus
Category:
Protein Pathway
Sub-Categories:
Gene Regulatory
Kinase Signaling
Cellular Response
Created: 2018-08-31
Last Updated: 2019-08-16
Insulin is responsible for the regulation of glucose levels in the body. It stimulates the storage of energy and inhibits the breakdown of high energy metabolites. Glycogen and lipid biosynthesis are upregulated, and conversely, glycogen and fatty acid metabolism are down-regulated. Insulin also modulates transcription and translation. Binding of insulin to the insulin receptor (IR) results in the activation of its tyrosine kinase activity leading to IR autophosphorylation. IR then phosphorylates several substrates that lead to the activation of an intracellular signalling cascade. IR activation leads to the activation of H-Ras, MAPK1-3, and PI3-kinase pathways. The activation of these pathways leads to modulation of key proteins in glycogen metabolism/lipid metabolism and transcription/translation.
References
Insulin Signalling References
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
Matsui Y, Kikuchi A, Kawata M, Kondo J, Teranishi Y, Takai Y: Molecular cloning of smg p21B and identification of smg p21 purified from bovine brain and human platelets as smg p21B. Biochem Biophys Res Commun. 1990 Jan 30;166(2):1010-6. doi: 10.1016/0006-291x(90)90911-6.
Pubmed: 2105724
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
Kawajiri A, Itoh N, Fukata M, Nakagawa M, Yamaga M, Iwamatsu A, Kaibuchi K: Identification of a novel beta-catenin-interacting protein. Biochem Biophys Res Commun. 2000 Jul 5;273(2):712-7. doi: 10.1006/bbrc.2000.3002.
Pubmed: 10873669
Emery AC, Eiden MV, Mustafa T, Eiden LE: Rapgef2 connects GPCR-mediated cAMP signals to ERK activation in neuronal and endocrine cells. Sci Signal. 2013 Jun 25;6(281):ra51. doi: 10.1126/scisignal.2003993.
Pubmed: 23800469
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
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 SMP0000391
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