Glycogen synthase kinase-3 beta activity is critical for neuronal death caused by inhibiting phosphatidylinositol 3-kinase or Akt but not for death caused by nerve growth factor withdrawal. (Q54415298)

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English	Glycogen synthase kinase-3 beta activity is critical for neuronal death caused by inhibiting phosphatidylinositol 3-kinase or Akt but not for death caused by nerve growth factor withdrawal.	scientific article

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scholarly article

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/10954722

Glycogen synthase kinase-3 beta activity is critical for neuronal death caused by inhibiting phosphatidylinositol 3-kinase or Akt but not for death caused by nerve growth factor withdrawal. (English)

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/10954722

author name string

R J Crowder

1

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/10954722

R S Freeman

2

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/10954722

language of work or name

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publication date

1 November 2000

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Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/10954722

Journal of Biological Chemistry

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Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/10954722

275

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/10954722

44

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/10954722

34266-34271

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/10954722

Neurotrophin signal transduction in the nervous system

1 reference

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Activation of phosphatidylinositol 3-kinase by epidermal growth factor, basic fibroblast growth factor, and nerve growth factor in PC12 pheochromocytoma cells

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Regulation of neuronal survival by the serine-threonine protein kinase Akt

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Inhibition of phosphatidylinositol 3-kinase activity blocks depolarization- and insulin-like growth factor I-mediated survival of cerebellar granule cells

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In sympathetic but not sensory neurones, phosphoinositide-3 kinase is important for NGF-dependent survival and the retrograde transport of 125I-betaNGF.

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Neuroprotection by brain-derived neurotrophic factor is mediated by extracellular signal-regulated kinase and phosphatidylinositol 3-kinase.

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Depolarization and neurotrophins converge on the phosphatidylinositol 3-kinase-Akt pathway to synergistically regulate neuronal survival

1 reference

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Cellular survival: a play in three Akts

1 reference

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Akt phosphorylation of BAD couples survival signals to the cell-intrinsic death machinery

1 reference

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Akt promotes cell survival by phosphorylating and inhibiting a Forkhead transcription factor

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Regulation of cell death protease caspase-9 by phosphorylation

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Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B

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Role of glycogen synthase kinase-3 in the phosphatidylinositol 3-Kinase/Akt cell survival pathway

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Axin and Frat1 interact with dvl and GSK, bridging Dvl to GSK in Wnt-mediated regulation of LEF-1.

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GBP, an inhibitor of GSK-3, is implicated in Xenopus development and oncogenesis

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Glycogen synthase kinase-3 and dorsoventral patterning in Xenopus embryos

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Nerve growth factor-induced PKB/Akt activity is sustained by phosphoinositide 3-kinase dependent and independent signals in sympathetic neurons

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Expression of a constitutively active Akt Ser/Thr kinase in 3T3-L1 adipocytes stimulates glucose uptake and glucose transporter 4 translocation

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Activation of a novel proto-oncogene, Frat1, contributes to progression of mouse T-cell lymphomas

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Suppression of glycogen synthase kinase activity is not sufficient for leukemia enhancer factor-1 activation

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A GSK3-binding peptide from FRAT1 selectively inhibits the GSK3-catalysed phosphorylation of axin and beta-catenin

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A molecular mechanism for the effect of lithium on development

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Lithium inhibits glycogen synthase kinase-3 activity and mimics wingless signalling in intact cells

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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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Interaction of axin and Dvl-2 proteins regulates Dvl-2-stimulated TCF-dependent transcription.

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The axis-inducing activity, stability, and subcellular distribution of beta-catenin is regulated in Xenopus embryos by glycogen synthase kinase 3

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Destabilization of beta-catenin by mutations in presenilin-1 potentiates neuronal apoptosis

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Phosphorylation of insulin receptor substrate 1 by glycogen synthase kinase 3 impairs insulin action

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Insulin receptor substrate (IRS)-1 and IRS-2 are tyrosine-phosphorylated and associated with phosphatidylinositol 3-kinase in response to brain-derived neurotrophic factor in cultured cerebral cortical neurons

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Lithium reduces tau phosphorylation by inhibition of glycogen synthase kinase-3.

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Opposing effects of ERK and JNK-p38 MAP kinases on apoptosis

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Blocking cytochrome c activity within intact neurons inhibits apoptosis.

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Regulation of NF-κB activity in rat dorsal root ganglia and PC12 cells by tumour necrosis factor and nerve growth factor

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Selective activation of NF-kappa B by nerve growth factor through the neurotrophin receptor p75.

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Nerve growth factor activates a Ras-dependent protein kinase that stimulates c-fos transcription via phosphorylation of CREB.

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Tumor necrosis factor induces Bcl-2 and Bcl-x expression through NFkappaB activation in primary hippocampal neurons

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Rel-dependent induction of A1 transcription is required to protect B cells from antigen receptor ligation-induced apoptosis

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21 January 2018

Identifiers

10.1074/JBC.M006160200

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/10954722

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

29 May 2018

http://europepmc.org/abstract/MED/10954722

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