ISOLATION OF A G-PROTEIN THAT IS MODIFIED BY LEARNING AND REDUCES POTASSIUM CURRENTS IN HERMISSENDA

被引:88
作者
NELSON, TJ
COLLIN, C
ALKON, DL
机构
[1] Laboratory of Molecular and Cellular Neurobiology, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda
关键词
D O I
10.1126/science.2108498
中图分类号
O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];
学科分类号
07 ; 0710 ; 09 ;
摘要
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.
引用
收藏
页码:1479 / 1483
页数:5
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