N-terminal acetylation targets GTPases to membranes.

N-terminal acetylation targets GTPases to membranes.
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N 末端乙酰化将 GTP 酶靶向膜。

DOI:
10.1038/ncb0504-379
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发表时间:
2004
影响因子:
21.3
通讯作者:
Jackson,CatherineL
Jackson,CatherineL
中科院分区:
生物学1区
文献类型:
--
作者:
Jackson,CatherineL

文献摘要

相似文献

小gtp酶Arl3p和Arl1p依次发挥作用,将各种效应蛋白招募到高尔基体。与ARF蛋白类似,Arl1p通过肉豆蔻酰化作用靶向细胞膜。然而,Arl3p不是肉豆蔻酰化的。最近的研究表明,Arl3p及其哺乳动物同源物ARFRP1通过氨基末端乙酰化作用靶向膜,从而促进膜受体Sys1p/hSys1的识别。
The small GTPases Arl3p and Arl1p function sequentially to recruit diverse effector proteins to the Golgi apparatus. Similarly to ARF proteins, Arl1p is targeted to membranes by myristoylation. Arl3p, however, is not myristoylated. Recent work demonstrates that Arl3p, and its mammalian orthologue ARFRP1, are targeted to membranes by amino-terminal acetylation, which facilitates recognition by the membrane receptor Sys1p/hSys1.