C-terminal phosphorylation of LKB1 is not required for regulation of AMP-activated protein kinase, BRSK1, BRSK2, or cell cycle arrest. - Wikidata - awgldk - TriplyDB

C-terminal phosphorylation of LKB1 is not required for regulation of AMP-activated protein kinase, BRSK1, BRSK2, or cell cycle arrest.

C-terminal phosphorylation of LKB1 is not required for regulation of AMP-activated protein kinase, BRSK1, BRSK2, or cell cycle arrest.

http://www.wikidata.org/entity/Q34852643

about

14-3-3 interacts with LKB1 via recognizing phosphorylated threonine 336 residue and suppresses LKB1 kinase function Fyn-dependent regulation of energy expenditure and body weight is mediated by tyrosine phosphorylation of LKB1 AMP-activated protein kinase: an energy sensor that regulates all aspects of cell function Uncoupling of the LKB1-AMPKalpha energy sensor pathway by growth factors and oncogenic BRAF Investigation of LKB1 Ser431 phosphorylation and Cys433 farnesylation using mouse knockin analysis reveals an unexpected role of prenylation in regulating AMPK activity LKB1 is an essential regulator of spermatozoa release during spermiation in the mammalian testis Histological evaluation of AMPK signalling in primary breast cancer Mechanism and role of high density lipoprotein-induced activation of AMP-activated protein kinase in endothelial cells.Targeted therapies of the LKB1/AMPK pathway for the treatment of insulin resistance β-Subunit myristoylation is the gatekeeper for initiating metabolic stress sensing by AMP-activated protein kinase (AMPK).Bile acid stimulates hepatocyte polarization through a cAMP-Epac-MEK-LKB1-AMPK pathway.Polarized activities of AMPK and BRSK in primary hippocampal neurons.Metformin accelerates the growth of BRAF V600E-driven melanoma by upregulating VEGF-A.Resveratrol as a calorie restriction mimetic: therapeutic implications.Post-translational modification of serine/threonine kinase LKB1 via Adduction of the Reactive Lipid Species 4-Hydroxy-trans-2-nonenal (HNE) at lysine residue 97 directly inhibits kinase activity Visualization of Compartmentalized Kinase Activity Dynamics Using Adaptable BimKARs.Phosphorylation of serine 399 in LKB1 protein short form by protein kinase Cζ is required for its nucleocytoplasmic transport and consequent AMP-activated protein kinase (AMPK) activation Hepatocyte polarity Identification of the serine 307 of LKB1 as a novel phosphorylation site essential for its nucleocytoplasmic transport and endothelial cell angiogenesis.Adiponectin activates AMP-activated protein kinase in muscle cells via APPL1/LKB1-dependent and phospholipase C/Ca2+/Ca2+/calmodulin-dependent protein kinase kinase-dependent pathways.Perivascular fat, AMP-activated protein kinase and vascular diseases.Role of AMPK throughout meiotic maturation in the mouse oocyte: evidence for promotion of polar body formation and suppression of premature activation.The LKB1 complex-AMPK pathway: the tree that hides the forest LKB1 and AMPK: central regulators of lymphocyte metabolism and function.Role of AMP-activated protein kinase in cancer therapy.Metabolic effects of resveratrol: addressing the controversies.Current evidence for AMPK activation involvement on resveratrol-induced neuroprotection in cerebral ischemia.Mechanisms of Paradoxical Activation of AMPK by the Kinase Inhibitors SU6656 and Sorafenib.AMPK Causes Cell Cycle Arrest in LKB1-Deficient Cells via Activation of CAMKK2 The role of AMP-activated protein kinase in quercetin-induced apoptosis of HL-60 cells.Nootkatone, a characteristic constituent of grapefruit, stimulates energy metabolism and prevents diet-induced obesity by activating AMPK.Regulation of Rac1 by simvastatin in endothelial cells: differential roles of AMP-activated protein kinase and calmodulin-dependent kinase kinase-beta.A comparison of LKB1/AMPK/mTOR metabolic axis response to global ischaemia in brain, heart, liver and kidney in a rat model of cardiac arrest.

P2860

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P2860

C-terminal phosphorylation of LKB1 is not required for regulation of AMP-activated protein kinase, BRSK1, BRSK2, or cell cycle arrest.

http://www.wikidata.org/entity/Q34852643

description

2008 nî lūn-bûn

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2008 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2008 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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C-terminal phosphorylation of ...... , BRSK2, or cell cycle arrest.

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C-terminal phosphorylation of ...... , BRSK2, or cell cycle arrest.

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C-terminal phosphorylation of ...... , BRSK2, or cell cycle arrest.

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C-terminal phosphorylation of ...... , BRSK2, or cell cycle arrest.

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C-terminal phosphorylation of ...... , BRSK2, or cell cycle arrest.

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C-terminal phosphorylation of ...... , BRSK2, or cell cycle arrest.

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C-terminal phosphorylation of ...... , BRSK2, or cell cycle arrest.

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C-terminal phosphorylation of ...... , BRSK2, or cell cycle arrest.

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Journal of Biological Chemistry

P1476

C-terminal phosphorylation of ...... , BRSK2, or cell cycle arrest.

@en

P2093

D Grahame Hardie

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Sarah Fogarty

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P2860

Complexes between the LKB1 tumor suppressor, STRAD alpha/beta and MO25 alpha/beta are upstream kinases in the AMP-activated protein kinase cascade

Structural basis for AMP binding to mammalian AMP-activated protein kinase

MO25alpha/beta interact with STRADalpha/beta enhancing their ability to bind, activate and localize LKB1 in the cytoplasm

Identification of the sucrose non-fermenting related kinase SNRK, as a novel LKB1 substrate

Activation of the tumour suppressor kinase LKB1 by the STE20-like pseudokinase STRAD

LKB1 is a master kinase that activates 13 kinases of the AMPK subfamily, including MARK/PAR-1

The regulation of AMP-activated protein kinase by phosphorylation

CBS domains form energy-sensing modules whose binding of adenosine ligands is disrupted by disease mutations

Phosphorylation of the protein kinase mutated in Peutz-Jeghers cancer syndrome, LKB1/STK11, at Ser431 by p90(RSK) and cAMP-dependent protein kinase, but not its farnesylation at Cys(433), is essential for LKB1 to suppress cell vrowth

Characterization of the AMP-activated protein kinase kinase from rat liver and identification of threonine 172 as the major site at which it phosphorylates AMP-activated protein kinase

P304

77-84

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scholarly article

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10.1074/JBC.M806152200

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P433

1

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P478

284

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2008-10-14T00:00:00Z

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phosphorylation

P932

2610510

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