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Deactivation of a negative regulator: a distinct signal transduction mechanism,
pronounced in Akt signaling
#MMPMID25418317
Rahman A
; Haugh JM
Biophys J
2014[Nov]; 107
(10
): L29-32
PMID25418317
show ga
Kinase cascades, in which enzymes are sequentially activated by phosphorylation,
are quintessential signaling pathways. Signal transduction is not always achieved
by direct activation, however. Often, kinases activate pathways by deactivation
of a negative regulator; this indirect mechanism, pervasive in Akt signaling, has
yet to be systematically explored. Here, we show that the indirect mechanism has
properties that are distinct from direct activation. With comparable parameters,
the indirect mechanism yields a broader range of sensitivity to the input, beyond
saturation of regulator phosphorylation, and kinetics that become progressively
slower, not faster, with increasing input strength. These properties can be
integrated in network motifs to produce desired responses, as in the case of
feedforward loops.
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