Investigation of Ldb19/Art1 localization and function at the late Golgi.

Investigation of Ldb19/Art1 localization and function at the late Golgi.
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LDB19/ART1在高尔基人晚期的定位和功能的研究。

DOI:
10.1371/journal.pone.0206944
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发表时间:
2018
期刊:
影响因子:
3.7
通讯作者:
Duncan MC
Duncan MC
中科院分区:
综合性期刊3区
文献类型:
--
作者:
Martínez-Márquez JY;Duncan MC

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Arrestin相关蛋白家族(ARTs)是酿酒酵母(Saccharomycescerevisiae)中多个细胞位置的膜运输的有效调节剂。几种ART在多个位置起作用,这表明在一个位置具有良好功能的ART可能在细胞的其他位置具有额外的,迄今为止,未表征的作用。为了更全面地了解ART蛋白调控的细胞功能谱,我们探索了Ldb 19/Art 1的定位和功能,Ldb 19/Art 1先前已被证明在质膜上起作用,但据报道定位于trans-Golgi网络(TGN)。我们报告说,Ldb 19与GFP的C-末端融合是功能性的,如前所述,定位于TGN。我们进一步确定Ldb 19与富含网格蛋白衔接蛋白复合物-1(AP-1)的TGN成熟晚期相关。此外,我们目前的遗传相互作用分析表明,Ldb 19的行为在后期TGN的机制相关的AP-1。然而,Ldb 19和AP-1在膜交通测定的子集中具有不同的表型,表明Ldb 19在TGN的功能与AP-1的功能不同。总之,这些结果表明,Ldb 19功能在TGN,除了其在胞吞作用中的作用。
The arrestin-related family of proteins (ARTs) are potent regulators of membrane traffic at multiple cellular locations in the yeast Saccharomyces cerevisiae. Several ARTs act at multiple locations, suggesting that ARTs with well-established functions at one location may have additional, as of yet, uncharacterized roles at other locations in the cell. To more fully understand the spectrum of cellular functions regulated by ART proteins, we explored the localization and function of Ldb19/Art1, which has previously been shown to function at the plasma membrane, yet is reported to localize to the trans-Golgi network (TGN). We report that the C-terminal fusion of Ldb19 with GFP is functional and, as previously reported, localizes to the TGN. We further establish that Ldb19 associates with late stages of TGN maturation that are enriched in the clathrin adaptor protein complex-1 (AP-1). Additionally, we present genetic interaction assays that suggest Ldb19 acts at the late TGN in a mechanism related to that of AP-1. However, Ldb19 and AP-1 have dissimilar phenotypes in a subset of assays of membrane traffic, suggesting Ldb19 functions at the TGN are distinct from those of AP-1. Together these results indicate Ldb19 functions at the TGN, in addition to its well-established role in endocytosis.
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