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In G2/M phase, PKC-ßII translocates to the nucleus, where
it is proposed to stimulate disassembly of the nuclear lamina by
phosphorylating lamin B1. But PKC-ßII is just one
of a host of cellular PKC isoforms. How do cells selectively translocate
PKC-ßII? Janet Lord and co-workers have addressed this
question by analysing the levels of potential PKC-activating lipids in nuclei
during the cell cycle; they used centrifugal elutriation to isolate cells at
different stages of the cell cycle and thereby avoid the use of cell cycle
inhibitors. The authors find that nuclear translocation of
PKC-ßII correlates with an increase in the levels of nuclear
diacylglycerol - in particular the tetraunsaturated species 1-stearoyl,
2-arachidonyl glycerol (SAG). They show that SAG potently activates
PKC-
and PKC-ßII but not the novel isoform PKC-
.
Lord and co-workers propose that generation of nuclear SAG at G2/M facilitates
association of PKC-ßII with the nuclear membrane - perhaps as
part of a general mechanism for differential control of PKC signalling by
distinct forms of diacylglycerol.
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