(Q24296738)

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A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain

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A method to identify serine kinase substrates. Akt phosphorylates a novel adipocyte protein with a Rab GTPase-activating protein (GAP) domain (English)

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phosphorylation

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AKT serine/threonine kinase 1

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GOA release 2020-03-11

protein phosphorylation

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GOA release 2020-03-11

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4

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John M Asara

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Susan Kane

1

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Hiroyuki Sano

2

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Simon C H Liu

3

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William S Lane

5

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Charles C Garner

6

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Gustav E Lienhard

7

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language of work or name

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publication date

21 June 2002

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Journal of Biological Chemistry

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277

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25

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22115-8

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A role for protein kinase Bbeta/Akt2 in insulin-stimulated GLUT4 translocation in adipocytes

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Differential effects of phosphatidylinositol 3-kinase inhibition on intracellular signals regulating GLUT4 translocation and glucose transport

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Role of S6 phosphorylation and S6 kinase in cell growth

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Sortilin is the major 110-kDa protein in GLUT4 vesicles from adipocytes

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GLUT4--at the cross roads between membrane trafficking and signal transduction

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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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Characterization of GAPCenA, a GTPase activating protein for Rab6, part of which associates with the centrosome

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Rab proteins as membrane organizers

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Insulin resistance and a diabetes mellitus-like syndrome in mice lacking the protein kinase Akt2 (PKB beta)

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Dephosphorylation of perilipin by protein phosphatases present in rat adipocytes

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7 January 2021

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10.1074/JBC.C200198200

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

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Consolidated OpenCitations Corpus – April 2017

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