Trends in Biochemical Sciences
Not all Shc's roads lead to Ras
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P66Shc Deletion Ameliorates Oxidative Stress and Cardiac Dysfunction in Pressure Overload-Induced Heart Failure
2020, Journal of Cardiac FailureCitation Excerpt :In this research, we were interested in the p66Shc protein. In mice, ShcA locus encodes 3 different isoforms through alternative splicing; among which p66Shc is the longest isoform.5 The tyrosine-phosphorylated p66Shc is a downstream molecule of growth factors.7
SIRT1 in cardiovascular aging
2014, Clinica Chimica ActaAdapter protein Shc regulates Janus kinase 3 phosphorylation
2014, Journal of Biological ChemistryCross-talk between integrin receptor and insulin-like growth factor receptor in regulation of collagen biosynthesis in cultured fibroblasts
2013, Advances in Medical SciencesCitation Excerpt :The best known IGF-IR signaling is phosphatidylinositol pathway leading to activation of Akt and transcription factors which stimulate expression of genes involved in the metabolism and transport of carbohydrates, protein biosynthesis and apoptosis [3,4,5]. Another IGF-IR-dependent signal transduction is the Ras-Raf-dependent pathway of MAP-kinase activation through the proteins Shc, GRB-2 and Sos [6]. Activation of this pathway leads to induction of transcription factors that stimulate gene expression of proteins regulating cell growth and differentiation.
The p66<sup>Shc</sup> gene paves the way for healthspan: Evolutionary and mechanistic perspectives
2013, Neuroscience and Biobehavioral ReviewsP66<sup>ShcA</sup>: Linking Mammalian Longevity with Obesity-Induced Insulin Resistance
2013, Vitamins and HormonesCitation Excerpt :The p46 and p52Shc isoforms have been implicated in mitogenic signaling and oncogenesis, by assisting receptor tyrosine kinase activity. Upon GF stimulation, these proteins are rapidly and efficiently tyrosine phosphorylated by all the tyrosine kinase receptors tested and have been found to recruit the Grb2/Sos complex to a membrane-proximal localization where it activates the Ras and the downstream MAP kinase cascade (Bonfini et al., 1996; Giorgetti, Pelicci, Pelicci, & Van Obberghen, 1994; Okada et al., 1997). Although p66Shc can be phosphorylated on tyrosine and interacts with GRb2, unlike p46 and p52, it has been shown to inhibit activation of the Ras/MAP kinase pathway triggered by the EGF and IGF-1 receptors, as well as by cytokines in lymphocytes (Migliaccio et al., 1997; Okada et al., 1997; Pacini et al., 2004).
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L. Bonfinl, E. Migliacclo, G. Pellcci, L. Lanfrancone and P. G. Pellccl are at the European Institute of Oncology, via Ripamonti 435, 20141 Milan, Italy.