G4296

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关键词:'G4296'

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Phosphorylated Rho-GDP directly activates mTORC2 kinase towards AKT through dimerization with Ras-GTP to regulate cell migration.

Hiroshi Senoo et al.

Nature cell biology, 21(7), 867-878 (2019-07-03)

mTORC2 plays critical roles in metabolism, cell survival and actin cytoskeletal dynamics through the phosphorylation of AKT. Despite its importance to biology and medicine, it is unclear how mTORC2-mediated AKT phosphorylation is controlled. Here, we identify an unforeseen principle by

Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signalling.

C Sutherland et al.

The Biochemical journal, 296 ( Pt 1), 15-19 (1993-11-15)

The beta-isoform of glycogen synthase kinase-3 (GSK3 beta) isolated from rabbit skeletal muscle was inactivated 90-95% following incubation with MgATP and either MAP kinase-activated protein kinase-1 (MAPKAP kinase-1, also termed RSK-2) or p70 S6 kinase (p70S6K), and re-activated with protein

A FBXO7/EYA2-SCFFBXW7 axis promotes AXL-mediated maintenance of mesenchymal and immune evasion phenotypes of cancer cells.

Shen, et al.

Molecular Cell, 82, 1123-1139 (2023)

The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling.

C A Grimes et al.

Progress in neurobiology, 65(4), 391-426 (2001-08-31)

Glycogen synthase kinase-3beta (GSK3beta) is a fascinating enzyme with an astoundingly diverse number of actions in intracellular signaling systems. GSK3beta activity is regulated by serine (inhibitory) and tyrosine (stimulatory) phosphorylation, by protein complex formation, and by its intracellular localization. GSK3beta

β-Catenin is a pH sensor with decreased stability at higher intracellular pH.

Katharine A White et al.

The Journal of cell biology, 217(11), 3965-3976 (2018-10-14)

β-Catenin functions as an adherens junction protein for cell-cell adhesion and as a signaling protein. β-catenin function is dependent on its stability, which is regulated by protein-protein interactions that stabilize β-catenin or target it for proteasome-mediated degradation. In this study

Requirement for glycogen synthase kinase-3beta in cell survival and NF-kappaB activation.

K P Hoeflich et al.

Nature, 406(6791), 86-90 (2000-07-14)

Glycogen synthase kinase-3 (GSK-3)-alpha and -beta are closely related protein-serine kinases, which act as inhibitory components of Wnt signalling during embryonic development and cell proliferation in adult tissues. Insight into the physiological function of GSK-3 has emerged from genetic analysis

Spreading of P301S Aggregated Tau Investigated in Organotypic Mouse Brain Slice Cultures.

Dhwani S Korde et al.

Biomolecules, 12(9) (2022-09-24)

Tau pathology extends throughout the brain in a prion-like fashion through connected brain regions. However, the details of the underlying mechanisms are incompletely understood. The present study aims to examine the spreading of P301S aggregated tau, a mutation that is

Glycogen synthase kinase-3 beta phosphorylates tau protein at multiple sites in intact cells.

B R Sperber et al.

Neuroscience letters, 197(2), 149-153 (1995-09-08)

Hyperphosphorylated tau protein is the major constituent of the paired helical filament (PHF), the major fibrous component of the neurofibrillary lesions of Alzheimer's disease (AD). Hyperphosphorylation of tau is believed to be the critical event that leads to filament assembly.

Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization.

J A Diehl et al.

Genes & development, 12(22), 3499-3511 (1998-12-01)

The activities of cyclin D-dependent kinases serve to integrate extracellular signaling during G1 phase with the cell-cycle engine that regulates DNA replication and mitosis. Induction of D-type cyclins and their assembly into holoenzyme complexes depend on mitogen stimulation. Conversely, the

The glamour and gloom of glycogen synthase kinase-3.

Richard S Jope et al.

Trends in biochemical sciences, 29(2), 95-102 (2004-04-23)

Glycogen synthase kinase-3 (GSK3) is now recognized as a key component of a surprisingly large number of cellular processes and diseases. Several mechanisms play a part in controlling the actions of GSK3, including phosphorylation, protein complex formation, and subcellular distribution.

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