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Pathway Description
Ras Signaling Pathway
Bos taurus
Category:
Protein Pathway
Sub-Categories:
Gene Regulatory
Kinase Signaling
Apoptosis Signaling
Cellular Response
Created: 2018-08-31
Last Updated: 2019-09-13
RAS signalling pathway is one of the main pathways to transduce intracellular signals in response to mitogens to controls cell growth, survival and anti-apoptotic programs. RAS proteins are GTP-binding proteins and must be bound to GTP to be active. Active RAS binds and activates effector enzymes that control cell proliferation, survival and other cell behaviours. RAS interacts directly with the catalytic subunit of PI3K to activate lipid kinases controlling the activity of downstream enzymes. Some of these kinases have anti-apoptotic activity, playing an important role in the survival signal of RAS. PI3K is also involved in the regulation of the actin cytoskeleton and transcription factor pathways. RAS also effects exchange factors causing inhibition of transcription factors from FoxO family, part of promoting cell cycle arrest and apoptosis. Normal function of these proteins require post-transcriptional modification. Pathway mutations in activation may result in human tumours.
References
Ras Signaling Pathway References
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Pubmed: 3143720
Kawata M, Kawahara Y, Sunako M, Araki S, Koide M, Tsuda T, Fukuzaki H, Takai Y: The molecular heterogeneity of the smg-21/Krev-1/rap1 proteins, a GTP-binding protein having the same effector domain as ras p21s, in bovine aortic smooth muscle membranes. Oncogene. 1991 May;6(5):841-8.
Pubmed: 1646988
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Pubmed: 19390049
Yamane HK, Farnsworth CC, Xie HY, Evans T, Howald WN, Gelb MH, Glomset JA, Clarke S, Fung BK: Membrane-binding domain of the small G protein G25K contains an S-(all-trans-geranylgeranyl)cysteine methyl ester at its carboxyl terminus. Proc Natl Acad Sci U S A. 1991 Jan 1;88(1):286-90. doi: 10.1073/pnas.88.1.286.
Pubmed: 1898776
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
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
Nakashima T, Higa H, Matsubara H, Benson AM, Yasunobu KT: The amino acid sequence of bovine heart cytochrome c. J Biol Chem. 1966 Mar 10;241(5):1166-77.
Pubmed: 5933874
Lee I, Salomon AR, Yu K, Doan JW, Grossman LI, Huttemann M: New prospects for an old enzyme: mammalian cytochrome c is tyrosine-phosphorylated in vivo. Biochemistry. 2006 Aug 1;45(30):9121-8. doi: 10.1021/bi060585v.
Pubmed: 16866357
Yu H, Lee I, Salomon AR, Yu K, Huttemann M: Mammalian liver cytochrome c is tyrosine-48 phosphorylated in vivo, inhibiting mitochondrial respiration. Biochim Biophys Acta. 2008 Jul-Aug;1777(7-8):1066-71. doi: 10.1016/j.bbabio.2008.04.023. Epub 2008 Apr 22.
Pubmed: 18471988
Rottenberg S, Schmuckli-Maurer J, Grimm S, Heussler VT, Dobbelaere DA: Characterization of the bovine IkappaB kinases (IKK)alpha and IKKbeta, the regulatory subunit NEMO and their substrate IkappaBalpha. Gene. 2002 Oct 16;299(1-2):293-300. doi: 10.1016/s0378-1119(02)01011-9.
Pubmed: 12459277
Reyes RA, Cockerell GL: Increased ratio of bcl-2/bax expression is associated with bovine leukemia virus-induced leukemogenesis in cattle. Virology. 1998 Mar 1;242(1):184-92. doi: 10.1006/viro.1998.9029.
Pubmed: 9501056
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 SMP0063784
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