2010
Dynamic cross‐talk between PI3‐kinase/Akt and Ras/ERK pathways in EGF receptor signaling that can affect drug sensitivity in tumor cells
Aksamitiene E, Kiyatkin A, Hoek J. Dynamic cross‐talk between PI3‐kinase/Akt and Ras/ERK pathways in EGF receptor signaling that can affect drug sensitivity in tumor cells. The FASEB Journal 2010, 24: 715.2-715.2. DOI: 10.1096/fasebj.24.1_supplement.715.2.Peer-Reviewed Original ResearchPI3KRas/ERK pathwayPI3-kinase/AktPI3K activityEGF dose-dependent mannerNegative feedback loopAdaptor proteinMitogenic signalingU0126 inhibitorIndependent parallel pathwaysERK activityEGF receptorERK pathwayCell survivalK activityReciprocal crosstalkERK responseRecruitment mechanismsPhosphorylated ERKImmunoblot analysisEGF dosesERKAkt expressionSubcellular fractionsCancer cells
2003
Tyr-317 Phosphorylation Increases Shc Structural Rigidity and Reduces Coupling of Domain Motions Remote from the Phosphorylation Site as Revealed by Molecular Dynamics Simulations*
Suenaga A, Kiyatkin AB, Hatakeyama M, Futatsugi N, Okimoto N, Hirano Y, Narumi T, Kawai A, Susukita R, Koishi T, Furusawa H, Yasuoka K, Takada N, Ohno Y, Taiji M, Ebisuzaki T, Hoek JB, Konagaya A, Kholodenko BN. Tyr-317 Phosphorylation Increases Shc Structural Rigidity and Reduces Coupling of Domain Motions Remote from the Phosphorylation Site as Revealed by Molecular Dynamics Simulations*. Journal Of Biological Chemistry 2003, 279: 4657-4662. PMID: 14613932, DOI: 10.1074/jbc.m310598200.Peer-Reviewed Original ResearchConceptsPhosphotyrosine bindingTyr-317Shc phosphorylationSH2 domainC-terminal Src homology 2 domainSrc homology 2 domainRas/Raf/MEK/ERK pathwayShc adaptor proteinRaf/MEK/ERK pathwayMEK/ERK pathwayReceptor tyrosine kinasesShc functionPhosphorylated ShcPhosphorylation sitesAdaptor proteinLinker regionShcTyrosine kinaseERK pathwayMembrane receptorsPhosphorylationDomain motionMolecular dynamics simulationsNumerous partnersDomain coupling