Transformation by ras oncogene induces nuclear shift of protein kinase C.
We measured protein kinase C (PKC) activity in normal and ras-transformed Balb/3T3 fibroblasts; cytosolic and nuclear-associated PKC activity was determined either as phorbol ester binding, PKC-dependent phosphorylation of histone III-S, or phosphorylation of endogenous nuclear proteins. Results demonstrate that ras-transformed fibroblasts show down-regulation of cytosolic PKC accompanied by increase of nuclear-associated PKC. These results provide evidence linking transformation to PKC nuclear shift with consequent phosphorylation of nuclear proteins.
Chiarugi
V
V
Laboratory of Molecular Biology, University of Firenze, Italy.
Magnelli
L
L
Pasquali
F
F
Vannucchi
S
S
Bruni
P
P
Quattrone
A
A
Basi
G
G
Capaccioli
S
S
Ruggiero
M
M
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology*; D003600:Cytosol / Q000201:enzymology; D005347:Fibroblasts / Q000201:enzymology; D011905:Genes, ras; D007700:Kinetics; D051379:Mice; D008807:Mice, Inbred BALB C / Q000235:genetics*; D010703:Phorbol Esters / Q000378:metabolism; D010766:Phosphorylation; D011493:Protein Kinase C / Q000235:genetics*; D014170:Transformation, Genetic
D010703:Phorbol Esters; D011493:Protein Kinase C