Starheim Kristian K, Kalvik Thomas V, Bjørkøy Geir, Arnesen Thomas
Department of Molecular Biology, University of Bergen, N-5020 Bergen, Norway.
Department of Molecular Medicine and Cancer Research, Center of Molecular Inflammation Research, Norwegian University of Technology and Natural Sciences, N-7006 Trondheim, Norway.
Biosci Rep. 2017 Apr 28;37(2). doi: 10.1042/BSR20170066. Print 2017 Apr 30.
The organization of the Golgi apparatus (GA) is tightly regulated. Golgi stack scattering is observed in cellular processes such as apoptosis and mitosis, and has also been associated with disruption of cellular lipid metabolism and neurodegenerative diseases. Our studies show that depletion of the human N-α-acetyltransferase 30 (hNaa30) induces fragmentation of the Golgi stack in HeLa and CAL-62 cell lines. The GA associated GTPase ADP ribosylation factor related protein 1 (ARFRP1) was previously shown to require N-terminal acetylation for membrane association and based on its N-terminal sequence, it is likely to be a substrate of hNaa30. ARFRP1 is involved in endosome-to--Golgi network (TGN) traffic. We observed that ARFRP1 shifted from a predominantly -Golgi and TGN localization to localizing both Golgi and non-Golgi vesicular structures in hNaa30-depleted cells. However, we did not observe loss of membrane association of ARFRP1. We conclude that hNaa30 depletion induces Golgi scattering and induces aberrant ARFRP1 Golgi localization.
高尔基体（GA）的组织受到严格调控。在细胞凋亡和有丝分裂等细胞过程中可观察到高尔基体堆叠的分散，并且它还与细胞脂质代谢紊乱和神经退行性疾病有关。我们的研究表明，人类N-α-乙酰转移酶30（hNaa30）的缺失会导致HeLa和CAL-62细胞系中高尔基体堆叠的碎片化。之前已表明，与GA相关的GTP酶ADP核糖基化因子相关蛋白1（ARFRP1）的膜结合需要N端乙酰化，基于其N端序列，它很可能是hNaa30的底物。ARFRP1参与从内体到高尔基体网络（TGN）的运输。我们观察到，在hNaa30缺失的细胞中，ARFRP1从主要定位于高尔基体和TGN转变为同时定位于高尔基体和非高尔基体囊泡结构。然而，我们并未观察到ARFRP1的膜结合丧失。我们得出结论，hNaa30的缺失会导致高尔基体分散，并诱导ARFRP1在高尔基体的异常定位。
