Retrieval of resident late-Golgi membrane proteins from the prevacuolar compartment of Saccharomyces cerevisiae is dependent on the function of Grd19p.
Retrieval of resident late-Golgi membrane proteins from the prevacuolar compartment of Saccharomyces cerevisiae is dependent on the function of Grd19p.
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DOI：
10.1083/jcb.140.3.577
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发表时间：
1998-02-09
影响因子：
7.8
通讯作者：
Stevens, TH
中科院分区：
文献类型：
--
作者：
Voos, W;Stevens, TH
酿酒酵母 (TGN) 晚期高尔基体区室的动态囊泡转运过程需要专用机制来正确定位驻留膜蛋白。在这项研究中，我们报告了一个新基因GRD19的鉴定，该基因参与模型晚期高尔基体膜蛋白A-ALP（由二肽氨肽酶A [DPAP A]的胞质结构域与碱性磷酸酶[ALP]的跨膜和腔结构域融合组成）的定位，该蛋白定位于酵母TGN。 grd19 无效突变导致晚期高尔基体膜蛋白 A-ALP 和 Kex2p 快速错误定位到液泡。与之前发现的参与晚期高尔基体膜蛋白定位的基因相比，grd19 突变仅对液泡蛋白分选产生很小的影响。 TGN 和前液泡区室之间的羧肽酶 Y 分选受体 Vps10p 的循环在 grd19Δ 细胞中基本上不受影响。 A-ALP 运输的动力学测定表明，GRD19 参与了从液泡前区室回收 A-ALP 的过程。 GRD19 编码一种主要分布在胞质中的小亲水蛋白。在积累了夸张形式的前液泡区室 (vps27) 的酵母突变体中，观察到 Grd19p 定位于该区室。使用体外结合测定，发现 Grd19p 与 DPAP A 的胞质结构域发生物理相互作用。我们得出结论，Grd19p 是修复机制的一个组成部分，在液泡前区室的分选/出芽过程中，通过与某些 TGN 膜蛋白的胞质尾部直接相互作用发挥作用。
The dynamic vesicle transport processes at the late-Golgi compartment of Saccharomyces cerevisiae (TGN) require dedicated mechanisms for correct localization of resident membrane proteins. In this study, we report the identification of a new gene, GRD19, involved in the localization of the model late-Golgi membrane protein A-ALP (consisting of the cytosolic domain of dipeptidyl aminopeptidase A [DPAP A] fused to the transmembrane and lumenal domains of the alkaline phosphatase [ALP]), which localizes to the yeast TGN. A grd19 null mutation causes rapid mislocalization of the late-Golgi membrane proteins A-ALP and Kex2p to the vacuole. In contrast to previously identified genes involved in late-Golgi membrane protein localization, grd19 mutations cause only minor effects on vacuolar protein sorting. The recycling of the carboxypeptidase Y sorting receptor, Vps10p, between the TGN and the prevacuolar compartment is largely unaffected in grd19Δ cells. Kinetic assays of A-ALP trafficking indicate that GRD19 is involved in the process of retrieval of A-ALP from the prevacuolar compartment. GRD19 encodes a small hydrophilic protein with a predominantly cytosolic distribution. In a yeast mutant that accumulates an exaggerated form of the prevacuolar compartment (vps27), Grd19p was observed to localize to this compartment. Using an in vitro binding assay, Grd19p was found to interact physically with the cytosolic domain of DPAP A. We conclude that Grd19p is a component of the retrieval machinery that functions by direct interaction with the cytosolic tails of certain TGN membrane proteins during the sorting/budding process at the prevacuolar compartment.
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影响因子：
7.8
作者：
FRANZUSOFF, A;REDDING, K;SCHEKMAN, R
通讯作者：
SCHEKMAN, R
DOI：
10.1083/jcb.120.5.1123
发表时间：
1993-03
期刊：
The Journal of cell biology
影响因子：
--
作者：
Humphrey JS;Peters PJ;Yuan LC;Bonifacino JS
通讯作者：
Bonifacino JS
影响因子：
3.3
作者：
Horazdovsky, BF;Davies, BA;Emr, SD
通讯作者：
Emr, SD
DOI：
10.1083/jcb.119.6.1459
发表时间：
1992-12
期刊：
The Journal of cell biology
影响因子：
--
作者：
Cooper A;Bussey H
通讯作者：
Bussey H
影响因子：
64.5
作者：
MARCUSSON, EG;HORAZDOVSKY, BF;EMR, SD
通讯作者：
EMR, SD