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Science 23 March 1990:
Vol. 247. no. 4949, pp. 1479 - 1483
DOI: 10.1126/science.2108498
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Articles
Science, Vol 247, Issue 4949, 1479-1483
Copyright © 1990 by American Association for the Advancement of Science
Isolation of a G protein that is modified by learning and reduces potassium currents in Hermissenda
TJ Nelson,
C Collin,
and
DL Alkon
Laboratory of Molecular and Cellular Neurobiology, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.
In Hermissenda crassicornis conditioned to associate light and rotation, type B photoreceptor neurons exhibit pairing-specific decreases in the potassium currents IA and IK-Ca, which account for many of the behavioral changes elicited by associative conditioning. To determine which proteins are involved in storage of this memory, high-performance liquid chromatography was used to examine proteins from Hermissenda eyes. Conditioning-specific changes in four phosphoproteins were observed 24 hours after conditioning. One of these proteins, cp20, was purified to apparent homogeneity and found to be a G protein. When injected back into Hermissenda type B cells, cp20 reduced IK and IK-Ca in a manner indistinguishable from the reduction caused by conditioning, suggesting that this protein may play a crucial role in memory acquisition or retention.
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