Signal convergence on protein kinase A as a molecular correlate of learning.
The response of a reaction network composed of protein kinase A, calpain, and protein phosphatase to transient cAMP and Ca2+ signals was studied. An essential feature of signal convergence is that the regulatory subunit of cAMP-dissociated protein kinase A undergoes limited proteolysis by the Ca(2+)-activated proteinase calpain. A dynamic model of this system based on kinetic differential equations was built and simulated by computer. The system shows analogies to typical features of associative learning such as acquisition, contiguity detection, extinction, and memory decay, suggesting that these biochemical reactions may be part of the molecular mechanism of learning in Drosophila.
Aszódi
A
A
Institute for Enzymology, Hungarian Academy of Sciences, Budapest.
Müller
U
U
Friedrich
P
P
Spatz
H C
HC
D002154:Calpain / Q000378:metabolism; D003198:Computer Simulation; D000242:Cyclic AMP / Q000378:metabolism; D004789:Enzyme Activation; D066298:In Vitro Techniques; D007700:Kinetics; D007858:Learning / Q000502:physiology*; D008954:Models, Biological; D010749:Phosphoprotein Phosphatases / Q000378:metabolism; D011494:Protein Kinases / Q000378:metabolism*; D013997:Time Factors
D000242:Cyclic AMP; D011494:Protein Kinases; D010749:Phosphoprotein Phosphatases; D002154:Calpain