Two distinct populations of ARF bound to Golgi membranes
Two distinct populations of ARF bound to Golgi membranes
复制标题
与高尔基体膜结合的两个不同的 ARF 群体
DOI:
--
复制
发表时间:
1993
影响因子:
7.8
通讯作者:
J. E. Rothman
中科院分区:
文献类型:
--
作者:
J. Helms;David J. Palmer;J. E. Rothman
ADP-ribosylation factor (ARF) is a small molecular weight GTP-binding protein (20 kD) and has been implicated in vesicular protein transport. The guanine nucleotide, bound to ARF protein is believed to modulate the activity of ARF but the mechanism of action remains elusive. We have previously reported that ARF binds to Golgi membranes after Brefeldin A-sensitive nucleotide exchange of ARF-bound GDP for GTP gamma S. Here we report that treatment with phosphatidylcholine liposomes effectively removed 40-60% of ARF bound to Golgi membranes with nonhydrolyzable GTP, presumably by competing for binding of activated ARF to lipid bilayers. This revealed the presence of two different pools of ARF on Golgi membranes. Whereas total ARF binding did not appear to be saturable, the liposome-resistant pool is saturable suggesting that this pool of ARF is stabilized by interaction with a Golgi membrane-component. We propose that activation of ARF by a guanine nucleotide-exchange protein results in association of myristoylated ARF GTP with the lipid bilayer of the Golgi apparatus. Once associated with the membrane, activated ARF can diffuse freely to associate stably with a target protein or possibly can be inactivated by a GTPase activating protein (GAP) activity.
DOI:
--
发表时间:
1982
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Northup,JK;Smigel,MD;Gilman,AG
通讯作者:
Gilman,AG
DOI:
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发表时间:
1990
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Clary,DO;Rothman,JE
通讯作者:
Rothman,JE
DOI:
--
发表时间:
1992
期刊:
The Journal of biological chemistry
影响因子:
--
作者:
Balch,WE;Kahn,RA;Schwaninger,R
通讯作者:
Schwaninger,R