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Answer:
a. Normally, PK2 activates PK1. We are told that PK1 and PK2 normally work sequentially in an intracellular signaling pathway. If PK1 is permanently activated, a response is seen independently of whether or not PK2 is present. If PK1 activated PK2, no response should be seen if PK1 were activated in the absence of PK2.
GSK-3 is an unusual protein kinase in that it displays high, “constitutive” activity in unstimulated cells and is rapidly inactivated upon a variety of cellular stimulations. The most thoroughly documented pathway for the inactivation of GSK-3 is in response to insulin and is mediated by protein kinase B (PKB, also termed Akt), which lies upstream of GSK-3 [8].
A cell wherein the PKB seems to be constantly active does indeed have a disorder that makes GSK3 to be permanently activated. Kinases, for example, control glycogen synthase as well as glucose acid phosphatase.
- GSK3, as well as glycogen synthase kinases 3, is however one enzyme that is controlled through PKB phosphorylase kinases.
- Throughout one cell, PKB seems to be constantly in motion, culminating in GSK3 regulation, which would, in turn, be responsible for glycogen synthase activities only through the signaling cascade.
Thus the response above is correct.
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