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Signal convergence on protein kinase A as a molecular correlate of learning.
Author(s) -
András Aszódi,
Uli Müller,
P. Friedrich,
H C Spatz
Publication year - 1991
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.13.5832
Subject(s) - calpain , protein subunit , contiguity , protein kinase a , proteolysis , microbiology and biotechnology , kinase , extinction (optical mineralogy) , phosphatase , convergence (economics) , biochemistry , chemistry , biology , biophysics , enzyme , gene , mineralogy , economics , ecology , economic growth
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.

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