Molecular evolution of the Rab-escort-protein/guanine-nucleotide-dissociation-inhibitor superfamily
Molecular evolution of the Rab-escort-protein/guanine-nucleotide-dissociation-inhibitor superfamily
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DOI：
10.1091/mbc.e03-04-0227
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发表时间：
2003-09-01
影响因子：
3.3
通讯作者：
Balch, WE
中科院分区：
文献类型：
--
作者：
Alory, C;Balch, WE
通过Rab香叶基香叶基转移酶（RabGGT酶）调节囊泡运输的Rab GTP酶的异戊烯化需要通过新合成的Rab蛋白与Rab护送蛋白（REP）的缔合形成的复合物，REP是在疾病中突变的无脉络膜基因产物，导致视力丧失。通过REP-Rab复合物递送至膜后，随后再循环至胞质溶胶需要REP相关的鸟嘌呤核苷酸解离抑制剂（GDI）。虽然REP和GDI具有共同的Rab结合特性，但GDI不能帮助Rab异戊烯化，REP不能从膜中检索Rab蛋白。我们现在已经分离出能够部分发挥REP和GDI功能的REP突变蛋白。这些结果提供了分子洞察REP/GDI超家族的功能和进化组织。
Prenylation of Rab GTPases regulating vesicle traffic by Rab geranylgeranyltransferase (RabGGTase) requires a complex formed by the association of newly synthesized Rab proteins with Rab-escort-protein (REP), the choroideremia-gene-product that is mutated in disease, leading to loss of vision. After delivery to the membrane by the REP-Rab complex, subsequent recycling to the cytosol requires the REP-related guanine-nucleotide-dissociation-inhibitor (GDI). Although REP and GDI share common Rab-binding properties, GDI cannot assist in Rab prenylation and REP cannot retrieve Rab proteins from the membranes. We have now isolated REP mutant proteins that are able to partially function as both REP and GDI. These results provide molecular insight into the functional and evolutionary organization of the REP/GDI superfamily.