Pertussis and cholera toxin ADP-ribosylation in Dictyostelium discoideum membranes.
Pertussis and cholera toxin ADP-ribosylation in Dictyostelium discoideum membranes.
复制标题
盘基网柄菌膜中的百日咳和霍乱毒素 ADP-核糖基化。
DOI：
10.1016/0006-291x(87)90504-3
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发表时间：
1987
影响因子：
3.1
通讯作者：
Howlett,A
中科院分区：
文献类型：
--
作者：
Khachatrian,L;Klein,C;Howlett,A
我们报告了一个39 kDa的霍乱和百日咳毒素底物存在于D。盘状突膜该蛋白不与对照哺乳动物细胞的Gs（45 kDa和52 kDa）或Gi（41 kDa）的α亚基共迁移。GTP或其非水解类似物的存在下，增强了ADP-核糖基化响应霍乱毒素，但没有显着改变ADP-核糖基化百日咳毒素。二价阳离子抑制ADP-核糖基化的毒素。这种新的G蛋白可能与D. discoideum腺苷酸环化酶可能是这种酶的一些独特调节特征的基础。或者，这种G蛋白可以调节由cAMP受体介导的几种其他细胞反应之一。
We report a 39 kDa substrate for cholera and pertussis toxins is present in D. discoideum membranes. This protein did not co-migrate with α subunits of either G s (45 kDa and 52 kDa) or G i (41 kDa) from control mammalian cells. The presence of GTP or its non-hydrolyzable analogs enhanced the ADP-ribosylation in response to cholera toxin, but did not significantly alter ADP-ribosylation by pertussis toxin. Divalent cations inhibited the ADP-ribosylation by both toxins. The possible association of this novel G-protein with D. discoideum adenylate cyclase may underlie some of the unique regulatory features of this enzyme. Alternatively, this G-protein may regulate one of several other cellular responses mediated by the cAMP receptor.