M. Passalacqua et al., Protein kinase C-theta is specifically localized on centrosomes and kinetochores in mitotic cells, BIOCHEM J, 337, 1999, pp. 113-118
In this study we provide evidence that the protein kinase C (PKC)-theta iso
enzyme is recruited on to the mitotic spindle in dividing murine erythroleu
kaemia (MEL) cells and associates specifically with centrosome and kinetoch
ore structures. None of the other PKC isoenzymes (-alpha, -delta, -epsilon,
-mu and -zeta) expressed by MEL cells shows this localization on the mitot
ic spindle. An identical subcellular distribution of PKC-theta is also obse
rved in dividing murine P3 myeloma cells and human LAN-5 neuroblastoma cell
s, indicating that this PKC isoenzyme interacts with the mitotic apparatus
in mammalian cells. In phorbol-ester-treated non-growing MEL cells, a rapid
change in the intracellular distribution of PKC-theta occurs. Under these
conditions, PKC-theta is translocated from the nuclear to the cytosolic cel
l compartment, an event that is accompanied by phosphorylation of the PKC-t
heta molecule and is followed by its down-regulation. The recovery of cell
growth capacity results in the concomitant reappearance of PKC-theta. Furth
ermore, when MEL cells acquire the differentiated non-growing phenotype, th
e level of PKC-theta is reduced to less than 5%, suggesting that this PKC i
soenzyme is no longer required. We propose that, unlike other members of th
e PKC family, PKC-theta may play a role in cell proliferation.