mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1) (Q24324148)

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English	mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1)	scientific article

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mTOR complex 2 (mTORC2) controls hydrophobic motif phosphorylation and activation of serum- and glucocorticoid-induced protein kinase 1 (SGK1) (English)

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phosphorylation

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mechanistic target of rapamycin kinase

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GOA release 2020-03-11

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object named as

Dario R Alessi

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author name string

Juan M García-Martínez

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language of work or name

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publication date

15 December 2008

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Biochemical Journal

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416

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3

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375-85

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Serum and glucocorticoid-regulated protein kinases: variations on a theme

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Defining the role of mTOR in cancer

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TOR signaling in growth and metabolism

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SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt phosphorylation and substrate specificity

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Direct inhibition of the longevity-promoting factor SKN-1 by insulin-like signaling in C. elegans

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Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton

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mSin1 is necessary for Akt/PKB phosphorylation, and its isoforms define three distinct mTORC2s

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Multiallelic disruption of the rictor gene in mice reveals that mTOR complex 2 is essential for fetal growth and viability

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Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not S6K1

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Prolonged rapamycin treatment inhibits mTORC2 assembly and Akt/PKB

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PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase

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mTOR-raptor binds and activates SGK1 to regulate p27 phosphorylation

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PDK1, the master regulator of AGC kinase signal transduction

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TSC2: filling the GAP in the mTOR signaling pathway

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Phosphoinositide-dependent protein kinase 1, a sensor of protein conformation

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mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the cell growth machinery

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Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action

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3-Phosphoinositide-dependent protein kinase-1 (PDK1): structural and functional homology with the Drosophila DSTPK61 kinase

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Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control

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Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive

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Regulation of TORC1 by Rag GTPases in nutrient response

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Binding of phosphatidylinositol 3,4,5-trisphosphate to the pleckstrin homology domain of protein kinase B induces a conformational change

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Exploitation of KESTREL to identify NDRG family members as physiological substrates for SGK1 and GSK3

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Identification of calcium-regulated heat-stable protein of 24 kDa (CRHSP24) as a physiological substrate for PKB and RSK using KESTREL.

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Ubiquitin-proteasome degradation of serum- and glucocorticoid-regulated kinase-1 (SGK-1) is mediated by the chaperone-dependent E3 ligase CHIP

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Identification of Protor as a novel Rictor-binding component of mTOR complex-2

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Role of phosphatidylinositol 3,4,5-trisphosphate in regulating the activity and localization of 3-phosphoinositide-dependent protein kinase-1

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Activation of serum- and glucocorticoid-regulated protein kinase by agonists that activate phosphatidylinositide 3-kinase is mediated by 3-phosphoinositide-dependent protein kinase-1 (PDK1) and PDK2

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WNK1 activates SGK1 to regulate the epithelial sodium channel.

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Molecular basis for the substrate specificity of NIMA-related kinase-6 (NEK6). Evidence that NEK6 does not phosphorylate the hydrophobic motif of ribosomal S6 protein kinase and serum- and glucocorticoid-induced protein kinase in vivo

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14-3-3 proteins modulate the expression of epithelial Na+ channels by phosphorylation-dependent interaction with Nedd4-2 ubiquitin ligase.

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PRR5, a novel component of mTOR complex 2, regulates platelet-derived growth factor receptor beta expression and signaling.

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Serum and glucocorticoid-inducible kinase (SGK) is a target of the PI 3-kinase-stimulated signaling pathway

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https://api.crossref.org/works/10.1042%2FBJ20081668

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The PIF-binding pocket in PDK1 is essential for activation of S6K and SGK, but not PKB.

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https://api.crossref.org/works/10.1042%2FBJ20081668

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Phosphorylation of Nedd4-2 by Sgk1 regulates epithelial Na(+) channel cell surface expression

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In vivo role of the PIF-binding docking site of PDK1 defined by knock-in mutation

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High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells

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Identification of Sin1 as an essential TORC2 component required for complex formation and kinase activity

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Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex

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The Rag GTPases bind raptor and mediate amino acid signaling to mTORC1

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Dual role of phosphatidylinositol-3,4,5-trisphosphate in the activation of protein kinase B

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Mutation of the PDK1 PH Domain Inhibits Protein Kinase B/Akt, Leading to Small Size and Insulin Resistance

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Protein kinase SGK mediates survival signals by phosphorylating the forkhead transcription factor FKHRL1 (FOXO3a)

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https://api.crossref.org/works/10.1042%2FBJ20081668

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Sgk kinases and their role in epithelial transport

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(Patho)physiological significance of the serum- and glucocorticoid-inducible kinase isoforms

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Pharmacologic characterization of a potent inhibitor of class I phosphatidylinositide 3-kinases.

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Impaired renal Na(+) retention in the sgk1-knockout mouse

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In vivo role of the phosphate groove of PDK1 defined by knockin mutation

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https://api.crossref.org/works/10.1042%2FBJ20081668

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The regulation of salt transport and blood pressure by the WNK-SPAK/OSR1 signalling pathway

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Intramolecular and intermolecular interactions of protein kinase B define its activation in vivo

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PRAS40 and PRR5-like protein are new mTOR interactors that regulate apoptosis.

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7 January 2021

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Identifiers

10.1042/BJ20081668

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Consolidated OpenCitations Corpus – April 2017

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OpenCitations bibliographic resource ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

PubMed publication ID

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Consolidated OpenCitations Corpus – April 2017

OpenCitations bibliographic resource ID

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