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

被引：62

作者：

Toda, K

Nogami, M

Murakami, K

Kanaho, Y

Nakayama, K ^{[1
]}

机构：

[1] Univ Tsukuba, Inst Biol Sci, Tsukuba, Ibaraki 3058572, Japan

[2] Univ Tsukuba, Inst Appl Biochem, Tsukuba, Ibaraki 3058572, Japan

[3] Tokyo Inst Technol, Dept Life Sci, Yokohama, Kanagawa 2268501, Japan

[4] Univ Tsukuba, Gene Expt Ctr, Tsukuba, Ibaraki 3058572, Japan

来源：

FEBS LETTERS | 1999年 / 442卷 / 2-3期

关键词：

ADP-ribosylation factor; endosome; lysosome; phospholipase D; vesicular transport;

D O I：

10.1016/S0014-5793(98)01646-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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, (C) 1999 Federation of European Biochemical Societies.

引用

页码：221 / 225

页数：5

共 29 条

[1] BIOSYNTHETIC TRANSPORT OF A MAJOR LYSOSOMAL MEMBRANE GLYCOPROTEIN, LAMP-1 - CONVERGENCE OF BIOSYNTHETIC AND ENDOCYTIC PATHWAYS OCCURS AT 3 DISTINCTIVE POINTS [J].