A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex.
A new role for RINT-1 in SNARE complex assembly at the trans-Golgi network in coordination with the COG complex.
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DOI：
10.1091/mbc.e13-01-0014
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发表时间：
2013-09
影响因子：
3.3
通讯作者：
Tagaya M
中科院分区：
文献类型：
--
作者：
Arasaki K;Takagi D;Furuno A;Sohda M;Misumi Y;Wakana Y;Inoue H;Tagaya M
酵母Tip20是DSL1复合体的一个亚单位，与高尔基体到内质网的逆行运输有关。与Tip20不同的是，哺乳动物中的Rint-1是内体到跨高尔基体网络运输所必需的。Rint-1与COG复合体协同调节SNARE复合体在跨高尔基体网络的组装。转运囊泡/载体与靶膜的对接和融合包括拴系因子介导的初始接触和可溶性N-乙基马来酰亚胺敏感因子附着蛋白受体(SNARE)催化的膜融合。多亚基拴系CATCHR家族复合体(DSL1、COG、外囊和GARP复合体)在亚基之间的序列同源性很低，尽管可能是从一个共同的祖先进化而来，并参与了根本不同的膜转运途径。酵母Tip20作为DSL1复合体的一个亚单位，参与了从高尔基体到内质网的逆行运输。我们以前的研究表明，酵母Tip20的哺乳动物对应基因Rint-1介导了ZW10(哺乳动物DSL1)与内质网定位的SNARE蛋白的联系。在目前的研究中，我们表明Rint-1也是内体到跨高尔基体网络运输所必需的。Rint-1与ZW10的非复合体与CATCHR家族复合体的另一个成员COG复合体相互作用，并调节SNARE复合体在跨高尔基体网络的组装。Rint-1的这种额外作用可能在一定程度上反映了与单细胞生物体酵母相比，哺乳动物对从内小体到跨高尔基体网络的运输途径更加多样化的需求。目前的发现突显了Rint-1在与COG复合体协调中的新作用。
Yeast Tip20, a subunit of the Dsl1 complex, is implicated in Golgi-to–endoplasmic reticulum retrograde transport. Differing from Tip20, its mammalian counterpart, RINT-1, is required for endosome-to–trans-Golgi network transport. RINT-1 in coordination with the COG complex regulates SNARE complex assembly at the trans-Golgi network. Docking and fusion of transport vesicles/carriers with the target membrane involve a tethering factor–mediated initial contact followed by soluble N-ethylmaleimide–sensitive factor attachment protein receptor (SNARE)–catalyzed membrane fusion. The multisubunit tethering CATCHR family complexes (Dsl1, COG, exocyst, and GARP complexes) share very low sequence homology among subunits despite likely evolving from a common ancestor and participate in fundamentally different membrane trafficking pathways. Yeast Tip20, as a subunit of the Dsl1 complex, has been implicated in retrograde transport from the Golgi apparatus to the endoplasmic reticulum. Our previous study showed that RINT-1, the mammalian counterpart of yeast Tip20, mediates the association of ZW10 (mammalian Dsl1) with endoplasmic reticulum–localized SNARE proteins. In the present study, we show that RINT-1 is also required for endosome-to–trans-Golgi network trafficking. RINT-1 uncomplexed with ZW10 interacts with the COG complex, another member of the CATCHR family complex, and regulates SNARE complex assembly at the trans-Golgi network. This additional role for RINT-1 may in part reflect adaptation to the demand for more diverse transport routes from endosomes to the trans-Golgi network in mammals compared with those in a unicellular organism, yeast. The present findings highlight a new role of RINT-1 in coordination with the COG complex.