Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1

J. Ann Le Good; Wolfgang H. Ziegler; Davey B. Parekh; Dario R. Alessi; Philip Cohen; Peter J. Parker

doi:10.1126/science.281.5385.2042

Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1

J. Ann Le Good, Wolfgang H. Ziegler, Davey B. Parekh, Dario R. Alessi, Philip Cohen, Peter J. Parker (Lead / Corresponding author)

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981 Citations (Scopus)

Abstract

Phosphorylation sites in members of the protein kinase A (PKA), PKG, and PKC kinase subfamily are conserved. Thus, the PKB kinase PDK1 may be responsible for the phosphorylation of PKC isotypes. PDK1 phosphorylated the activation loop sites of PKCζ and PKCδ in vitro and in a phosphoinositide 3-kinase (PI 3-kinase)-dependent manner in vivo in human embryonic kidney (293) cells. All members of the PKC family tested formed complexes with PDK1, PDK1-dependent phosphorylation of PKCδ in vitro was stimulated by combined PKC and PDK1 activators. The activation loop phosphorylation of PKCδ in response to serum stimulation of cells was PI 3-kinase-dependent and was enhanced by PDK1 coexpression.

Original language	English
Pages (from-to)	2042-2045
Number of pages	4
Journal	Science
Volume	281
Issue number	5385
DOIs	https://doi.org/10.1126/science.281.5385.2042
Publication status	Published - 25 Sept 1998

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title = "Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1",

abstract = "Phosphorylation sites in members of the protein kinase A (PKA), PKG, and PKC kinase subfamily are conserved. Thus, the PKB kinase PDK1 may be responsible for the phosphorylation of PKC isotypes. PDK1 phosphorylated the activation loop sites of PKCζ and PKCδ in vitro and in a phosphoinositide 3-kinase (PI 3-kinase)-dependent manner in vivo in human embryonic kidney (293) cells. All members of the PKC family tested formed complexes with PDK1, PDK1-dependent phosphorylation of PKCδ in vitro was stimulated by combined PKC and PDK1 activators. The activation loop phosphorylation of PKCδ in response to serum stimulation of cells was PI 3-kinase-dependent and was enhanced by PDK1 coexpression.",

author = "{Le Good}, {J. Ann} and Ziegler, {Wolfgang H.} and Parekh, {Davey B.} and Alessi, {Dario R.} and Philip Cohen and Parker, {Peter J.}",

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T1 - Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1

AU - Le Good, J. Ann

AU - Ziegler, Wolfgang H.

AU - Parekh, Davey B.

AU - Alessi, Dario R.

AU - Cohen, Philip

AU - Parker, Peter J.

PY - 1998/9/25

Y1 - 1998/9/25

N2 - Phosphorylation sites in members of the protein kinase A (PKA), PKG, and PKC kinase subfamily are conserved. Thus, the PKB kinase PDK1 may be responsible for the phosphorylation of PKC isotypes. PDK1 phosphorylated the activation loop sites of PKCζ and PKCδ in vitro and in a phosphoinositide 3-kinase (PI 3-kinase)-dependent manner in vivo in human embryonic kidney (293) cells. All members of the PKC family tested formed complexes with PDK1, PDK1-dependent phosphorylation of PKCδ in vitro was stimulated by combined PKC and PDK1 activators. The activation loop phosphorylation of PKCδ in response to serum stimulation of cells was PI 3-kinase-dependent and was enhanced by PDK1 coexpression.

AB - Phosphorylation sites in members of the protein kinase A (PKA), PKG, and PKC kinase subfamily are conserved. Thus, the PKB kinase PDK1 may be responsible for the phosphorylation of PKC isotypes. PDK1 phosphorylated the activation loop sites of PKCζ and PKCδ in vitro and in a phosphoinositide 3-kinase (PI 3-kinase)-dependent manner in vivo in human embryonic kidney (293) cells. All members of the PKC family tested formed complexes with PDK1, PDK1-dependent phosphorylation of PKCδ in vitro was stimulated by combined PKC and PDK1 activators. The activation loop phosphorylation of PKCδ in response to serum stimulation of cells was PI 3-kinase-dependent and was enhanced by PDK1 coexpression.

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Protein kinase C isotypes controlled by phosphoinositide 3-kinase through the protein kinase PDK1

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