Colocalization of phospholipase D1 and GTP‐binding‐defective mutant of ADP‐ribosylation factor 6 to endosomes and lysosomes

FEBS Letters

Murakami, Kazuo²  Nakayama, Kazuhisa¹  Nogami, Masahiro³  Kanaho, Yasunori³  Toda, Kyoko² 

[1] Institute of Biological Sciences, University of Tsukuba, Tsukuba Science City, Ibaraki 305-8572, Japan;Institute of Applied Biochemistry, University of Tsukuba, Tsukuba Science City, Ibaraki 305-8572, Japan;Department of Life Science, Tokyo Institute of Technology, Nagatsuda, Yokohama 226-8501, Japan

关键词: ADP-ribosylation factor;    Endosome;    Lysosome;    Phospholipase D;    Vesicular transport;    PLD;    phospholipase D;    PA;    phosphatidic acid;    ARF;    ADP-ribosylation factor;    GFP;    green fluorescent protein;    ER;    endoplasmic reticulum;    HA;    hemagglutinin;    Tfn-R;    transferrin receptor;    Man II;    mannosidase II;    BFA;    brefeldin A;   

DOI  :  10.1016/S0014-5793(98)01646-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Phospholipase D (PLD) is involved in various aspects of cellular function. Two isoforms, PLD1 and PLD2, have been identified. PLD1, which has two splicing variants, is regulated by various factors, including ADP-ribosylation factor (ARF). We here show that both variants of PLD1 are predominantly localized to late endosomes and lysosomes, but not to the Golgi apparatus or endoplasmic reticulum in contrast to earlier studies. Furthermore, PLD1s show significant colocalization with an ARF6 mutant defective in GTP binding. The data suggest that PLD1, under the regulation of ARF6, plays a role in the function of endosomes and lysosomes.

【 授权许可】

Unknown