AtRMR1 functions as a cargo receptor for protein trafficking to the protein storage vacuole.
AtRMR1 functions as a cargo receptor for protein trafficking to the protein storage vacuole.
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DOI：
10.1083/jcb.200504112
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发表时间：
2005-08-29
期刊：
影响因子：
--
通讯作者：
Hwang I
中科院分区：
文献类型：
--
作者：
Park M;Lee D;Lee GJ;Hwang I
细胞器蛋白质在到达其最终目的地的途中被货物受体分类。然而，蛋白质的受体是注定的蛋白质储存泡（PSV）在很大程度上是未知的。在这项研究中，我们调查的生物学作用，拟南芥受体同源区跨膜结构域环H2基序蛋白（AtRMR）1在蛋白质运输到PSV发挥。AtRMR 1主要定位于PSV的前液泡区室，但也有一小部分定位于高尔基复合体。AtRMR 1突变体定位于高尔基复合体的共表达强烈抑制了菜豆蛋白向PSV的运输，并导致菜豆蛋白在高尔基复合体或其分泌物中的积累。免疫共沉淀和体外结合试验表明，AtRMR 1的内腔域相互作用的COOH-末端分选信号的菜豆蛋白在酸性pH值。此外，菜豆蛋白共定位与AtRMR 1的方式的PSV。基于这些结果，我们建议，AtRMR 1的功能作为分选受体的菜豆蛋白的运输到PSV。
Organellar proteins are sorted by cargo receptors on the way to their final destination. However, receptors for proteins that are destined for the protein storage vacuole (PSV) are largely unknown. In this study, we investigated the biological role that Arabidopsis thaliana receptor homology region transmembrane domain ring H2 motif protein (AtRMR) 1 plays in protein trafficking to the PSV. AtRMR1 mainly colocalized to the prevacuolar compartment of the PSV, but a minor portion also localized to the Golgi complex. The coexpression of AtRMR1 mutants that were localized to the Golgi complex strongly inhibited the trafficking of phaseolin to the PSV and caused accumulation of phaseolin in the Golgi complex or its secretion. Coimmunoprecipitation and in vitro binding assays revealed that the lumenal domain of AtRMR1 interacts with the COOH-terminal sorting signal of phaseolin at acidic pH. Furthermore, phaseolin colocalized with AtRMR1 on its way to the PSV. Based on these results, we propose that AtRMR1 functions as the sorting receptor of phaseolin for its trafficking to the PSV.
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