Mutation of the PDK1 PH Domain Inhibits Protein Kinase B/Akt, Leading to Small Size and Insulin Resistance
about
AMIGO2, a novel membrane anchor of PDK1, controls cell survival and angiogenesis via Akt activation.Akt1 intramitochondrial cycling is a crucial step in the redox modulation of cell cycle progressionGenetic and Pharmacological Inhibition of PDK1 in Cancer Cells: CHARACTERIZATION OF A SELECTIVE ALLOSTERIC KINASE INHIBITORUbiquitin-specific protease 4 inhibits mono-ubiquitination of the master growth factor signaling kinase PDK1Requirement of 3-phosphoinositide-dependent protein kinase-1 for BDNF-mediated neuronal survivalInvestigation of LKB1 Ser431 phosphorylation and Cys433 farnesylation using mouse knockin analysis reveals an unexpected role of prenylation in regulating AMPK activityPhysical association of PDK1 with AKT1 is sufficient for pathway activation independent of membrane localization and phosphatidylinositol 3 kinasePhosphoinositide-dependent protein kinase (PDK) activity regulates phosphatidylinositol 3,4,5-trisphosphate-dependent and -independent protein kinase B activation and chemotaxisTargeting SGK1 in diabetesA novel inhibitor of the PI3K/Akt pathway based on the structure of inositol 1,3,4,5,6-pentakisphosphate.Discovery of small molecule inhibitors of the PH domain leucine-rich repeat protein phosphatase (PHLPP) by chemical and virtual screening.The physiological impact of the serum and glucocorticoid-inducible kinase SGK1PDK1 regulates vascular remodeling and promotes epithelial-mesenchymal transition in cardiac development.Angiotensin-induced EGF receptor transactivation inhibits insulin signaling in C9 hepatic cells.The kinase PDK1 is essential for B-cell receptor mediated survival signaling.Protein kinase B controls transcriptional programs that direct cytotoxic T cell fate but is dispensable for T cell metabolism.Multiple implications of 3-phosphoinositide-dependent protein kinase 1 in human cancer.Regulation of skeletal muscle growth by the IGF1-Akt/PKB pathway: insights from genetic models.Inhibition of HIV-1 Tat-mediated transcription by a coumarin derivative, BPRHIV001, through the Akt pathway.PI3K/Akt signaling requires spatial compartmentalization in plasma membrane microdomains.miR-155 Controls Lymphoproliferation in LAT Mutant Mice by Restraining T-Cell Apoptosis via SHIP-1/mTOR and PAK1/FOXO3/BIM PathwaysRole of TAPP1 and TAPP2 adaptor binding to PtdIns(3,4)P2 in regulating insulin sensitivity defined by knock-in analysis.Phosphatidylserine binding is essential for plasma membrane recruitment and signaling function of 3-phosphoinositide-dependent kinase-1.Alternative Activation Mechanisms of Protein Kinase B Trigger Distinct Downstream Signaling Responses.Phosphoinositide-dependent kinase-1 and protein kinase Cδ contribute to endothelin-1 constriction and elevated blood pressure in intermittent hypoxiaPhosphatidylinositol-3,4,5-triphosphate and cellular signaling: implications for obesity and diabetes.Interaction of PDK1 with phosphoinositides is essential for neuronal differentiation but dispensable for neuronal survivalAkt regulates L-type Ca2+ channel activity by modulating Cavalpha1 protein stability.Ku-0063794 is a specific inhibitor of the mammalian target of rapamycin (mTOR)Cross talk between the Akt and p38α pathways in macrophages downstream of Toll-like receptor signaling.3-Phosphoinositide-dependent kinase 1 potentiates upstream lesions on the phosphatidylinositol 3-kinase pathway in breast carcinoma.New insights into the regulation and function of serine/threonine kinases in T lymphocytes.Hepatic gluconeogenesis is enhanced by phosphatidic acid which remains uninhibited by insulin in lipodystrophic Agpat2-/- mice.Phosphoinositide 3-kinase and the mammalian target of rapamycin pathways control T cell migrationAkt isoforms and glucose homeostasis - the leptin connection.Metabolism, migration and memory in cytotoxic T cells.The coordination of T-cell function by serine/threonine kinases.Regulation of glucose metabolism in T cells: new insight into the role of Phosphoinositide 3-kinases.Serine-threonine kinases in TCR signaling.Transcription factors and cognate signalling cascades in the regulation of autophagy.
P2860
Q27309773-4D263ABE-72E7-493D-A322-564D9822EA12Q27339328-E06DE597-AB68-4315-A886-8224396227E5Q27666122-EF81A475-F68B-4B54-A3D0-6654E4AE7393Q28480531-C293BD25-AACD-4659-8156-AD5FDF8D86B1Q28565877-E1398B6F-E8DE-4DFF-A657-25A49B254B64Q28591614-1402AC06-832B-43E4-A65F-A64380B5F9F5Q28748305-8FEDB7DC-36D1-47A8-A393-92323ECC9521Q30493503-AA5250EC-96E6-4CF4-87F1-A38A7084CBFEQ33560146-7A9133AC-E0DF-43C9-BB6E-8F6E4A27718AQ33620076-2A684CCB-F020-4BEE-B4FF-423CB119B173Q33690795-663B016B-AE2B-4025-B35C-943D8DA967FEQ33904863-2D25F40B-7F63-412B-A105-FD5AE6C57E41Q33963861-ABD847B2-FAD9-44FA-95E2-0FE26AC23569Q34180196-DD21DA82-9D48-45F2-B6F9-E2C38263C87CQ34580922-270406CD-142B-4747-9A21-5983D0241C8FQ34641201-12C37EC2-D79C-4190-BB89-8968540D9BD6Q34878940-093B4FEC-5039-438F-8E32-F20B8F33BD4BQ35128706-ED1DB565-8FEF-41BC-949F-68BDD7908EB1Q35192970-4144EBC0-6523-4F73-8C60-3A4949E7E15EQ35197975-E8983C02-75A5-4958-94BB-BCAD7AD11E36Q35676981-D67F886E-9288-45C1-85C8-612C2CC837AEQ35707657-3F96355A-6C40-40BD-8113-2AB4DDAE4406Q35842095-ADB52AB3-3493-4377-B524-8ED073BCECA4Q36139887-42D0A837-119C-431F-8A53-0192809629FEQ36497577-180CBFA9-6C0B-468E-A4FE-FA665F964F7CQ36702291-92751508-8373-47F0-BF0E-FBDB949E543EQ36757048-F0558855-1251-4D75-AEFC-CB6BD1099A38Q37234352-19B2EF2F-C703-4925-82DE-E5E69C1D7106Q37257487-E94FBAB3-58DF-44D0-8598-F94D2EB748D6Q37265027-D6769E6C-89C8-4E2D-82B3-1D3EF7ED6349Q37307044-EBF2563D-0516-4B7C-ACFA-2E442490C1BAQ37416272-F7B3A462-DCF1-494F-BA33-A99989B41814Q37596317-DAEA4E6F-AABF-4B53-B70A-FE6457183107Q37690383-D733E8F2-5FD3-4766-9052-4EDD1D410D01Q37800267-49A83F98-D230-4320-A62D-0B0FA8DAC786Q37828371-1BB3F8C4-02D1-471E-8A55-25D956E5CEBCQ37855336-AB3C77A0-F1E9-4334-990D-8EA9E5DECEE4Q38034501-E7D898E5-D3AA-4778-AD03-3981B958B48CQ38241274-A6D63774-3245-4073-991B-31A243E02FCAQ38344277-A10444B2-4004-4668-BFED-9F8EB37B6151
P2860
Mutation of the PDK1 PH Domain Inhibits Protein Kinase B/Akt, Leading to Small Size and Insulin Resistance
description
2008 nî lūn-bûn
@nan
2008 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
Mutation of the PDK1 PH Domain ...... ll Size and Insulin Resistance
@ast
Mutation of the PDK1 PH Domain ...... ll Size and Insulin Resistance
@en
Mutation of the PDK1 PH Domain ...... ll Size and Insulin Resistance
@nl
type
label
Mutation of the PDK1 PH Domain ...... ll Size and Insulin Resistance
@ast
Mutation of the PDK1 PH Domain ...... ll Size and Insulin Resistance
@en
Mutation of the PDK1 PH Domain ...... ll Size and Insulin Resistance
@nl
prefLabel
Mutation of the PDK1 PH Domain ...... ll Size and Insulin Resistance
@ast
Mutation of the PDK1 PH Domain ...... ll Size and Insulin Resistance
@en
Mutation of the PDK1 PH Domain ...... ll Size and Insulin Resistance
@nl
P2093
P2860
P50
P356
P1476
Mutation of the PDK1 PH domain ...... ll size and insulin resistance
@en
P2093
Carol Clacher
David Komander
Florian Lang
Janna A van Diepen
John A Chudek
Juan M García-Martínez
Kei Sakamoto
Krishna M Boini
Peter J Voshol
Stephan Wullschleger
P2860
P304
P356
10.1128/MCB.02032-07
P407
P50
P577
2008-03-17T00:00:00Z