Insulin activates protein kinase B, inhibits glycogen synthase kinase‐3 and activates glycogen synthase by rapamycin‐insensitive pathways in skeletal muscle and adipose tissue

[1]  D. Turnbull,et al.  Insulin action in cultured human myoblasts: contribution of different signalling pathways to regulation of glycogen synthesis. , 1996, The Biochemical journal.

[2]  E. Van Obberghen,et al.  Different effects of insulin and platelet-derived growth factor on phosphatidylinositol 3-kinase at the subcellular level in 3T3-L1 adipocytes. A possible explanation for their specific effects on glucose transport. , 1996, European journal of biochemistry.

[3]  A. Depaoli-Roach,et al.  Regulation of Both Glycogen Synthase and PHAS-I by Insulin in Rat Skeletal Muscle Involves Mitogen-activated Protein Kinase-independent and Rapamycin-sensitive Pathways (*) , 1996, The Journal of Biological Chemistry.

[4]  P. Cohen,et al.  Inhibition of glycogen synthase kinase-3 by insulin mediated by protein kinase B , 1995, Nature.

[5]  Y. Le Marchand-Brustel,et al.  Insulin Stimulation of Mitogen-activated Protein Kinase, p90rsk, and p70 S6 Kinase in Skeletal Muscle of Normal and Insulin-resistant Mice , 1995, The Journal of Biological Chemistry.

[6]  Philip R. Cohen,et al.  Comparison of the specificities of p70 S6 kinase and MAPKAP kinase‐1 identifies a relatively specific substrate for p70 S6 kinase: the N‐terminal kinase domain of MAPKAP kinase‐1 is essential for peptide phosphorylation , 1995, FEBS letters.

[7]  Philip R. Cohen,et al.  PD 098059 Is a Specific Inhibitor of the Activation of Mitogen-activated Protein Kinase Kinase in Vitro and in Vivo(*) , 1995, The Journal of Biological Chemistry.

[8]  P. Cohen,et al.  Phosphotyrosine residues in the nerve-growth-factor receptor (Trk-A). Their role in the activation of inositolphospholipid metabolism and protein kinase cascades in phaeochromocytoma (PC12) cells. , 1995, European journal of biochemistry.

[9]  N. J. Edgell,et al.  Multiple signalling pathways involved in the stimulation of fatty acid and glycogen synthesis by insulin in rat epididymal fat cells. , 1995, The Biochemical journal.

[10]  P. Cuatrecasas,et al.  Mitogen-activated Protein Kinase Kinase Inhibition Does Not Block the Stimulation of Glucose Utilization by Insulin (*) , 1995, The Journal of Biological Chemistry.

[11]  R. Roth,et al.  Insulin stimulates the kinase activity of RAC‐PK, a pleckstrin homology domain containing ser/thr kinase. , 1995, The EMBO journal.

[12]  B. Burgering,et al.  Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction , 1995, Nature.

[13]  K. Siddle,et al.  Insulin stimulation of glycogen synthesis and glycogen synthase activity is blocked by wortmannin and rapamycin in 3T3-L1 adipocytes: evidence for the involvement of phosphoinositide 3-kinase and p70 ribosomal protein-S6 kinase. , 1995, The Biochemical journal.

[14]  C. Proud,et al.  Wortmannin inhibits the effects of insulin and serum on the activities of glycogen synthase kinase-3 and mitogen-activated protein kinase. , 1994, The Biochemical journal.

[15]  J. Lawrence,et al.  Activation of ribosomal protein S6 kinases does not increase glycogen synthesis or glucose transport in rat adipocytes. , 1994, The Journal of biological chemistry.

[16]  Ivan Dikic,et al.  PC12 cells overexpressing the insulin receptor undergo insulin-dependent neuronal differentiation , 1994, Current Biology.

[17]  P. Cohen,et al.  EGF triggers neuronal differentiation of PC12 cells that overexpress the EGF receptor , 1994, Current Biology.

[18]  P. Cohen,et al.  The α‐isoform of glycogen synthase kinase‐3 from rabbit skeletal muscle is inactivated by p70 S6 kinase or MAP kinase‐activated protein kinase‐1 in vitro , 1994, FEBS letters.

[19]  P. Cohen,et al.  Inactivation of glycogen synthase kinase-3 beta by phosphorylation: new kinase connections in insulin and growth-factor signalling. , 1993, The Biochemical journal.

[20]  C. Proud,et al.  Glycogen synthase kinase-3 is rapidly inactivated in response to insulin and phosphorylates eukaryotic initiation factor eIF-2B. , 1993, The Biochemical journal.

[21]  P. Cohen,et al.  Purification and characterisation of the insulin-stimulated protein kinase from rabbit skeletal muscle; close similarity to S6 kinase II. , 1991, European journal of biochemistry.

[22]  P. Dent,et al.  The molecular mechanism by which insulin stimulates glycogen synthesis in mammalian skeletal muscle , 1990, Nature.

[23]  P. Cohen,et al.  Evidence for communication between nerve growth factor and protein tyrosine phosphorylation , 1990, FEBS letters.

[24]  P. Cohen,et al.  Regulation of protein phosphatase-1G from rabbit skeletal muscle. 2. Catalytic subunit translocation is a mechanism for reversible inhibition of activity toward glycogen-bound substrates. , 1989, European journal of biochemistry.

[25]  W. Benjamin,et al.  Insulin action rapidly decreases multifunctional protein kinase activity in rat adipose tissue. , 1988, The Journal of biological chemistry.

[26]  P. Cohen,et al.  The protein phosphatases involved in cellular regulation. Purification and characterisation of the glycogen-bound form of protein phosphatase-1 from rabbit skeletal muscle. , 1985, European journal of biochemistry.

[27]  P. Cohen,et al.  Glycogen synthase from rabbit skeletal muscle; effect of insulin on the state of phosphorylation of the seven phosphoserine residues in vivo. , 2005, European journal of biochemistry.

[28]  P. Cohen,et al.  The purification and properties of rabbit skeletal muscle glycogen synthase. , 1976, European journal of biochemistry.

[29]  M. M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.