How the occupied KDEL receptor ERD2 is sorted into COPI vesicles for Golgi-to-ER transport is largely unknown. Here, interactions between proteins of the COPI transport machinery occurring during a "wave" of transport of a KDEL ligand were studied in living cells. FRET between CFP and YFP fusion proteins was measured by multifocal multiphoton microscopy and bulk-cell spectrofluorimetry. Ligand binding induces oligomerization of ERD2 and recruitment of ARFGAP to the Golgi, where the (ERD2)n/ARFGAP complex interacts with membrane-bound ARF1. During KDEL ligand transport, interactions of ERD2 with beta-COP and p23 decrease and the proteins segregate. Both p24a and p23 interact with ARF1, but only p24 interacts with ARFGAP. These findings suggest a model for how cargo-induced oligomerization of ERD2 regulates its sorting into COPI-coated buds.

译文

如何将占据的KDEL受体ERD2分类为COPI囊泡以进行高尔基体到ER运输,目前尚不清楚。在这里,在活细胞中研究了KDEL配体转运 “波” 过程中发生的COPI转运机制蛋白质之间的相互作用。CFP和YFP融合蛋白之间的FRET通过多焦点多光子显微镜和体细胞荧光光谱法测量。配体结合诱导ERD2的低聚和ARFGAP向高尔基体的募集,其中 (ERD2)n/ARFGAP复合物与膜结合的arf1相互作用。在KDEL配体转运过程中,ERD2与 β-COP和p23的相互作用降低,蛋白质分离。p24a和p23都与ARF1相互作用,但只有p24与ARFGAP相互作用。这些发现为cargo诱导的ERD2寡聚化如何调节其分选为COPI包被的芽提供了一个模型。

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