Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain
Structural basis of ubiquitin recognition by mammalian Eap45 GLUE domain
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DOI：
10.1038/nsmb1163
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发表时间：
2006-11-01
影响因子：
16.8
通讯作者：
Wakatsuki, Soichi
中科院分区：
文献类型：
--
作者：
Hirano, Satoshi;Suzuki, Nobuhiro;Wakatsuki, Soichi
ESCRT-II是一种将泛素化膜蛋白分类到溶酶体的复合物，通过Vps 36亚基的GLUE结构域和磷脂酰肌醇（PI）之间的相互作用定位到内体。在酵母中，泛素（Ub）相互作用的NZF结构域插入Vps 36 GLUE中，而其哺乳动物对应物Eap 45 GLUE缺乏NZF结构域。在Eap 45 GLUE-Ub复合物结构中，Ub的结合位点远离Eap 45 GLUE的PI结合位点，表明它们是独立结合的.
ESCRT-II, a complex that sorts ubiquitinated membrane proteins to lysosomes, localizes to endosomes through interaction between the Vps36 subunit's GLUE domain and phosphatidylinositides (PIs). In yeast, a ubiquitin (Ub) i nteracting NZF domain is inserted in Vps36 GLUE, whereas its mammalian counterpart, Eap45 GLUE, lacks the NZF domain. In the Eap45 GLUE - Ub complex structure, Ub binds far from the proposed PI- binding site of Eap45 GLUE, suggesting their independent binding.