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Research article

Activation of protein kinase B β and γ isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B α

Kay S. WALKER, Maria DEAK, Andrew PATERSON, Kevin HUDSON, Philip COHEN, Dario R. ALESSI
Biochemical Journal Apr 01, 1998, 331 (1) 299-308; DOI: 10.1042/bj3310299
Kay S. WALKER
MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee DD1 4HN, Scotland, U.K.
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  • For correspondence: kswalker@BAD.dundee.ac.uk
Maria DEAK
MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee DD1 4HN, Scotland, U.K.
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Andrew PATERSON
MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee DD1 4HN, Scotland, U.K.
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Kevin HUDSON
Zeneca Pharmaceuticals, Mereside, Alderley Park, Macclesfield, Cheshire SK10 4TG, U.K.
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Philip COHEN
MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee DD1 4HN, Scotland, U.K.
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Dario R. ALESSI
MRC Protein Phosphorylation Unit, Department of Biochemistry, University of Dundee, Dundee DD1 4HN, Scotland, U.K.
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Abstract

The regulatory and catalytic properties of the three mammalian isoforms of protein kinase B (PKB) have been compared. All three isoforms (PKBα, PKBβ and PKBγ) were phosphorylated at similar rates and activated to similar extents by 3-phosphoinositide-dependent protein kinase-1 (PDK1). Phosphorylation and activation of each enzyme required the presence of PtdIns(3,4,5)P3 or PtdIns(3,4)P2, as well as PDK1. The activation of PKBβ and PKBγ by PDK1 was accompanied by the phosphorylation of the residues equivalent to Thr308 in PKBα, namely Thr309 (PKBβ) and Thr305 (PKBγ). PKBγ which had been activated by PDK1 possessed a substrate specificity identical with that of PKBα and PKBβ towards a range of peptides. The activation of PKBγ and its phosphorylation at Thr305 was triggered by insulin-like growth factor-1 in 293 cells. Stimulation of rat adipocytes or rat hepatocytes with insulin induced the activation of PKBα and PKBβ with similar kinetics. After stimulation of adipocytes, the activity of PKBβ was twice that of PKBα, but in hepatocytes PKBα activity was four-fold higher than PKBβ. Insulin induced the activation of PKBα in rat skeletal muscle in vivo, with little activation of PKBβ. Insulin did not induce PKBγ activity in adipocytes, hepatocytes or skeletal muscle, but PKBγ was the major isoform activated by insulin in rat L6 myotubes (a skeletal-muscle cell line).

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April 1998

Volume: 331 Issue: 1

Biochemical Journal: 331 (1)
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Activation of protein kinase B β and γ isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B α
Kay S. WALKER, Maria DEAK, Andrew PATERSON, Kevin HUDSON, Philip COHEN, Dario R. ALESSI
Biochemical Journal Apr 1998, 331 (1) 299-308; DOI: 10.1042/bj3310299
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Activation of protein kinase B β and γ isoforms by insulin in vivo and by 3-phosphoinositide-dependent protein kinase-1 in vitro: comparison with protein kinase B α
Kay S. WALKER, Maria DEAK, Andrew PATERSON, Kevin HUDSON, Philip COHEN, Dario R. ALESSI
Biochemical Journal Apr 1998, 331 (1) 299-308; DOI: 10.1042/bj3310299

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