Coat-tether interaction in Golgi organization
Coat-tether interaction in Golgi organization
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DOI：
10.1091/mbc.e07-12-1236
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发表时间：
2008-07-01
影响因子：
3.3
通讯作者：
Linstedt, Adam D.
中科院分区：
文献类型：
--
作者：
Guo, Yusong;Punj, Vasu;Linstedt, Adam D.
高尔基体的生物发生可能是由COPI囊泡包被复合物介导的，但其机制尚不清楚。基于网格蛋白接头AP2的COPI亚基β COP建模表明，β COP C末端形成一个带有保守的FW结合口袋基序的附件结构域。在基因敲除后进行基因替换时，具有FW基序突变或侧翼基本残基的β COP版本在高尔基组织中产生缺陷，使人想起在缺乏囊泡系链p115时发生的缺陷。事实上，beta COP结合了p115，这取决于beta COP FW基序。此外，这种相互作用依赖于p115头部结构域的E19E21，反向电荷取代阻断了完整细胞中的高尔基体生物发生。最后，含有完整但未突变的β COP FW或p115 EE基序的抑制剂显著降低了渗透细胞中的高尔基体组装。因此，高尔基结构依赖于β COP和p115中相互作用的结构域，这表明高尔基体上的囊泡系结涉及p115与COPI外壳的结合。
Biogenesis of the Golgi apparatus is likely mediated by the COPI vesicle coat complex, but the mechanism is poorly understood. Modeling of the COPI subunit beta COP based on the clathrin adaptor AP2 suggested that the beta COP C terminus forms an appendage domain with a conserved FW binding pocket motif. On gene replacement after knockdown, versions of beta COP with a mutated FW motif or flanking basic residues yielded a defect in Golgi organization reminiscent of that occurring in the absence of the vesicle tether p115. Indeed, beta COP bound p115, and this depended on the beta COP FW motif. Furthermore, the interaction depended on E19E21 in the p115 head domain and inverse charge substitution blocked Golgi biogenesis in intact cells. Finally, Golgi assembly in permeabilized cells was significantly reduced by inhibitors containing intact, but not mutated, beta COP FW or p115 EE motifs. Thus, Golgi organization depends on mutually interacting domains in beta COP and p115, suggesting that vesicle tethering at the Golgi involves p115 binding to the COPI coat.