Phosphoinositide-dependent protein kinase-1 (PDK1)-independent activation of the protein kinase C substrate, protein kinase D

Autor: Sharon A. Matthews, April P. Kelly, Doreen A. Cantrell, C. David Wood
Rok vydání: 2007
Předmět:
animal structures
Biophysics
P70-S6 Kinase 1
Thymus Gland
Protein Serine-Threonine Kinases
Biology
Mitogen-activated protein kinase kinase
Biochemistry
Article
Cell Line
MAP2K7
3-Phosphoinositide-Dependent Protein Kinases
Mice
03 medical and health sciences
ES cell
embryonic stem cell
Structural Biology
PKC
protein kinase C
Genetics
Animals
ASK1
PKC
Molecular Biology
p90RSK
p90 ribosomal S6 kinase
Protein Kinase C
Protein kinase C
030304 developmental biology
Mice
Knockout
0303 health sciences
MAP kinase kinase kinase
PKD
030302 biochemistry & molecular biology
Cyclin-dependent kinase 2
Cell Biology
PDK1
3′-phosphoinositide-dependent protein kinase-1
S6K1
70-kilodalton ribosomal S6 kinase 1
3. Good health
Cell biology
Enzyme Activation
PKD
protein kinase D
PDK1
biology.protein
Cyclin-dependent kinase 9
Zdroj: Febs Letters
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2007.06.060
Popis: Phosphoinoisitide dependent kinase l (PDK1) is proposed to phosphorylate a key threonine residue within the catalytic domain of the protein kinase C (PKC) superfamily that controls the stability and catalytic competence of these kinases. Hence, in PDK1-null embryonic stem cells intracellular levels of PKCalpha, PKCbeta1, PKCgamma, and PKCepsilon are strikingly reduced. Although PDK1-null cells have reduced endogenous PKC levels they are not completely devoid of PKCs and the integrity of downstream PKC effector pathways in the absence of PDK1 has not been determined. In the present report, the PDK1 requirement for controlling the phosphorylation and activity of a well characterised substrate for PKCs, the serine kinase protein kinase D, has been examined. The data show that in embryonic stem cells and thymocytes loss of PDK1 does not prevent PKC-mediated phosphorylation and activation of protein kinase D. These results reveal that loss of PDK1 does not functionally inactivate all PKC-mediated signal transduction.
Databáze: OpenAIRE
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