Role of protein kinase B in insulin-regulated glucose uptake

Welsh, Gavin I.; Hers, Ingeborg; Berwick, Daniel C.; Dell, Ghislaine; Wherlock, Matthew; Birkin, R; Leney, Sophie E; Tavaré, Jeremy M.

doi:10.1042/bst0330346

Cited by 111 publications

(81 citation statements)

References 32 publications

(40 reference statements)

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“…In turn, PI(3,4,5)P3 functions to recruit and acivate atypical protein kinase C isoforms (PKCζ/λ) and the Akt protein kinases (sometimes referred to as (PKB) protein kinase B). Akt activation occurs through phosphorylation on threonine 308 by phosphoinositide-dependent protein kinase 1 (PDK1) and serine 473 by PDK2 [71][72][73]. Although there are three Akt isoforms, Akt2 function appears to be specifically required for insulin-stimulated GLUT4 translocation [73][74][75][76].…”

Section: Insulin Signaling Leading To Glut4 Translocationmentioning

confidence: 99%

Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

Hou

Pessin

2007

Current Opinion in Cell Biology

132

116

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SummaryGlucose transporter 4 (GLUT4) is the major insulin regulated glucose transporter expressed mainly in muscle and adipose tissue. GLUT4 is stored in a poorly characterized intracellular vesicular compartment and translocates to the cell surface in response to insulin stimulation resulting in increase glucose uptake. This process is essential for the maintenance of normal glucose homeostasis and involves a complex interplay of trafficking events and intracellular signaling cascades. Recent studies have identified sortilin as an essential element for the formation of GLUT4 storage vesicles during adipogenesis and GGA (Golgi-localized γ-ear-containing Arf-binding protein) as a key coat adaptor for the entry of newly synthesized GLUT4 into the specialized compartment. Insulinstimulated GLUT4 translocation from this compartment to the plasma membrane appears to require the Akt/protein kinase B substrate, termed AS160 (Akt Substrate of 160 kDa). In addition, the VPS9 domain-containing protein Gapex-5 in complex with CIP4 appears to function as a Rab31 guanylnucleotide exchange factor that is necessary for insulin-stimulated GLUT4 translocation. Here we attempt to summaries recent advances in GLUT4 vesicle biogenesis, intracellular trafficking and membrane fusion.

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Section: Insulin Signaling Leading To Glut4 Translocationmentioning

confidence: 99%

Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

Hou

Pessin

2007

Current Opinion in Cell Biology

132

116

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“…Following insulin receptor activation, Akt is phosphorylated at two residues (Ser 473 and Thr 308 ) crucial for activation (32,33). Insulin-stimulated phosphorylation of Akt at Ser 473 and Thr 308 was not affected by GIP (Fig.…”

Section: Gip Potentiates Insulin Action In Adipocytes-mentioning

confidence: 99%

Gastric Inhibitory Peptide Controls Adipose Insulin Sensitivity via Activation of cAMP-response Element-binding Protein and p110β Isoform of Phosphatidylinositol 3-Kinase

Mohammad

Ramos

Buck

et al. 2011

Journal of Biological Chemistry

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Background: GIP is a gut hormone secreted in response to nutrient intake. Results: GIP has an insulin-sensitizing effect on adipose via activation of the cAMP/PKA/CREB and p110␤ PI3K. Conclusion: These data define a novel signal transduction pathway modulating insulin action in adipocytes. Significance: Insulin-sensitizing activity points to a central role for GIP in coordinating intestinal nutrient sensing and regulation of metabolism.

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“…Insulin has been shown in other cell systems to activate the PI3-K pathway and thus stimulate glucose uptake by causing the translocation of insulin responsive GLUTs, such as GLUT4, to the plasma membrane (for review see Welsh et al 2005). It is controversial whether insulin-stimulation results in the activation of this pathway in preimplantation embryos.…”

Section: Introductionmentioning

confidence: 99%

Glucose utilization and the PI3-K pathway: mechanisms for cell survival in preimplantation embryos

Riley¹,

Moley²

2006

Reproduction

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The maintenance of optimal glucose utilization during the preimplantation period is critical for embryo survival. A decrease in glucose transport during preimplantation development has been linked to the early steps of programmed cell death in these embryos. Decreased glucose transport is not thought to be simply a consequence of cell death, rather it is thought to be a trigger that can initiate the apoptotic cascade. Extensive apoptosis during the preimplantation period may manifest later in pregnancy as a malformation -or miscarriage, if cell loss is excessive. Phosphatidylinositol 3-kinase (PI3-K) is a known regulator of a number of physiologic responses including cellular proliferation, growth, and survival as well as glucose metabolism. Studies performed in other cell systems have demonstrated that the PI3-K pathway plays a critical role in maintaining glucose transport and metabolism. This review will present the current evidence that suggests that PI3-K is vital for preimplantation embryo survival and development. In addition, data demonstrating that PI3-K activity is important for glucose metabolism during this early developmental period will be discussed.

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Role of protein kinase B in insulin-regulated glucose uptake

Cited by 111 publications

References 32 publications

Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

Ins (endocytosis) and outs (exocytosis) of GLUT4 trafficking

Gastric Inhibitory Peptide Controls Adipose Insulin Sensitivity via Activation of cAMP-response Element-binding Protein and p110β Isoform of Phosphatidylinositol 3-Kinase

Glucose utilization and the PI3-K pathway: mechanisms for cell survival in preimplantation embryos

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