Published online 7 August 2006. doi:10.1083/jcb.1744iti1
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 174, Number 4, 474-474
PKC decodes Ca2+
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Ca2+ waves are read out as waves of PKC translocation to the plasma membrane (shown).
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Movements of a swift kinase keep up with quick calcium bursts, based on findings of Reither et al. (page 521).
Cellular Ca2+ signals come in many flavorsfrom long-lasting global increases to waves to brief local plumes. Each flavor is translated into a specific cellular response by Ca2+ sensors, including calmodulin and conventional PKCs (cPKCs).
Upon Ca2+ binding, PKC
a common cPKCtranslocates to the plasma membrane, the location of most of its targets, including ion channels and transporters. The bulkiness of PKC
might suggest that its diffusion constants should be too low for rapidly following the fast and brief Ca2+ signals. Many researchers thus suspected that tiny calmodulin must be the main translator of these signals.
But the new findings reveal that PKC
is fleet footed. The authors found that PKC
's membrane translocation mimicsin both space and timethe full range of the cellular Ca2+ signals.
Just fractions of a second after a Ca2+ burst, PKC
was found at the membrane, where it lingered either for mere milliseconds or for longer stretches of several seconds. The short-lived membrane residence solely depended on cytosolic Ca2+. The more intimate interactions required PKC
's binding to the membrane lipid diacylglycerol (DAG). Since this binding is required for full activation of the kinase, the authors suspect that the shorter interactions might not necessarily lead to downstream signaling events.
Copies of PKC
that encounter Ca2+ in the center of the cell are unlikely ever to make it to the plasma membrane, as the Ca2+-PKC
complex is short lived. The authors thus suggest that PKC
activation depends solely on subplasma membrane Ca2+ signals. Perinuclear signals probably trigger an entirely different set of downstream eventsperhaps via calmodulin, which has many cytoplasmic substrates.
Nicole LeBrasseur
lebrasn{at}rockefeller.edu

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