Targeting of the arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p
Targeting of the arf-like GTPase Arl3p to the Golgi requires N-terminal acetylation and the membrane protein Sys1p
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DOI：
10.1038/ncb1120
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发表时间：
2004-05-01
影响因子：
21.3
通讯作者：
Munro, S
中科院分区：
文献类型：
--
作者：
Behnia, R;Panic, B;Munro, S
在酿酒酵母中，GTdR Arl 3 p需要募集第二个GTdR Arl 1 p到高尔基体。ArI 1 p与GRIP结构域结合，GRIP结构域存在于许多长卷曲螺旋蛋白或“golgins”中。在这里，我们表明，Arl 3 p是不豆蔻酰化的Arf家族的大多数成员一样，而是氨基末端乙酰化的NatC复合物。靶向Arl 3 p还需要高尔基体膜蛋白Sys 1 p。Arl 3 p（Arf相关蛋白1（ARFRP 1））和Sys 1 p（hSys 1）的人类同源物可以在化学交联后在复合物中分离。这表明ARFRP 1/Arl 3 p靶向高尔基体是由其乙酰化的N末端与Sys 1 p/hSys 1之间的直接相互作用介导的。
The GTPase Arl3p is required to recruit a second GTPase, ArI1p, to the Golgi in Saccharomyces cerevisiae. ArI1p binds to the GRIP domain, which is present in a number of long coiled-coil proteins or 'golgins'. Here we show that Arl3p is not myristoylated like most members of the Arf family, but is instead amino-terminally acetylated by the NatC complex. Targeting of Arl3p also requires a Golgi membrane protein Sys1p. The human homologues of Arl3p (Arf-related protein 1 (ARFRP1)) and Sys1p (hSys1) can be isolated in a complex after chemical cross-linking. This suggests that the targeting of ARFRP1/Arl3p to the Golgi is mediated by a direct interaction between its acetylated N terminus and Sys1p/hSys1.