M. Deak et al., Characterisation of a plant 3-phosphoinositide-dependent protein kinase-1 homologue which contains a pleckstrin homology domain, FEBS LETTER, 451(3), 1999, pp. 220-226
A plant homologue of mammalian 3-phosphoinositide-dependent protein kinase-
1 (PDK1) has been identified in Arabinopsis and rice which displays 40% ove
rall identity with human 3-phosphoinositide-dependent protein kinase-1. Lik
e the mammalian 3-phosphoinositide-dependent protein kinase-1, Arabidopsis
3-phosphoinositide-dependent protein kinase-1 and rice 3-phosphoinositide-d
ependent protein kinase-1 possess a kinase domain at N-termini and a plecks
trin homology domain at their C-termini, Arabidopsis 3-phosphoinositide-dep
endent protein kinase-1 can rescue lethality in Saccharomyces cerevisiae ca
used by disruption of the genes encoding yeast 3-phosphoinositide-dependent
protein kinase-1 homologues, Arabidopsis 3-phosphoinositide-dependent prot
ein kinase-1 interacts,ia its pleckstrin homology domain with phosphatidic
acid, PtdIns3P, PtdIns(3,4,5)P-3 and PtdIns(3,4)P-2 and to a lesser extent
with PtdIns(4,5)P-2 and PtdIns4P. Arabidopsis 3-phosphoinositide-dependent
protein kinase-1 is able to activate human protein kinase B alpha (PKB/AKT)
in the presence of PtdIns(3,4,5)P-3. Arabidopsis 3-phosphoinositide-depend
ent protein kinase-1 is only the second plant protein reported to possess a
pleckstrin homology domain and the first plant protein shown to bind 3-pho
sphoinositides. (C) 1999 Federation of European Biochemical Societies.