Phosphorylation and functional inactivation of TSC2 by Erk implications for tuberous sclerosis and cancer pathogenesis.

By Li Ma, Zhenbang Chen, H. Erdjument‐Bromage, Paul Tempst, P. Pandolfi. Cell, 2005

1,341 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology, Physiology

View Paper: https://www.semanticscholar.org/paper/07e0805c32f4e95e51ff723dcb2043a27c2daa7f

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Citations in the corpus

Activation and Function of the MAPKs and Their Substrates, the MAPK-Activated Protein Kinases (2011, background): “RSK and ERK phosphorylate TSC2 at Ser1798 and Ser664, respectively, which negatively regulates the guanine nucleotide-activating protein (GAP) activity of TSC2 toward the small GTPase Rheb (222, 291, 300).”
TOR signaling in growth and metabolism. (2006, positive): “Activated Erk1/2 directly phosphorylates TSC2 at sites that differ from the Akt target sites, thereby causing functional inactivation of the TSC1-TSC2 complex (Ma et al., 2005a).”
Regulation of mTORC1 by amino acids (2014, neutral): “The TSC complex, whose loss underlies a hamartomatous syndrome of the same name (17, 18), serves as a central hub for numerous extracellular and intracellular inputs including mitogen and growth factor signaling (19-23), energy levels (24), oxygen availability (25, 26) and genotoxic stress (27), whi”
Epidermal Growth Factor Receptor Cell Proliferation Signaling Pathways (2017, neutral): “ERK1/2 directly phosphorylates TSC2 on S664 [290].”
Translational control of long-lasting synaptic plasticity and memory. (2009, neutral): “(YXXXXLF, where X is any amino acid and F is a hydrophobic amino acid), through which they compete for binding to the convex dorsal surface of eIF4E (Mader et al., 1995; Marcotrigiano et al., 1999).”
The PTEN–PI3K pathway: of feedbacks and cross-talks (2008, positive): “Our group, along with the Cantley lab, recently demonstrated that Tsc2 heterozygous mice develop malignancies in which this feedback inhibition is overactive (Ma et al., 2005b; Manning et al., 2005).”
mTOR signaling in growth control and disease (2012, background): “…protein kinase B (Akt/PKB), extracellular-signal-regulated kinase 1/2 (ERK1/2), and ribosomal S6 kinase (RSK1)—directly phosphorylate the TSC1/TSC2 complex to inactivate it and thus activate mTORC1 (Inoki et al., 2002; Ma et al., 2005; Manning et al., 2002; Potter et al., 2002; Roux et al., 2004).”
Regulation of mTORC1 and its impact on gene expression at a glance (2013, background): “Active AKT promotes mTORC1 action by two means: (1) reducing the interaction of proline-rich AKT substrate 40 kDa (PRAS40) with mTORC1 (Sancak et al., 2007; Thedieck et al., 2007; Vander Haar et al., 2007; Wang et al., 2007), and (2) phosphorylating and inactivating the tuberous sclerosis complex (T”
The RAS/RAF/MEK/ERK and the PI3K/AKT signalling pathways: role in cancer pathogenesis and implications for therapeutic approaches (2012, background): “Indeed, ERK phosphorylation leads to TSC1/ TSC2 dissociation and impairs the ability of TSC2 to inhibit mTOR signalling [47].”
The mTOR Signalling Pathway in Human Cancer (2012, background): “ERK and RSK induce inhibitory phosphorylation of TSC2 at Ser664 and Ser1798 respectively, which promotes TSC1/TSC2 dissociation, which in turn leads to mTORC1 activation [80–82].”