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

作者信息

Toda K, Nogami M, Murakami K, Kanaho Y, Nakayama K

机构信息

Institute of Applied Biochemistry, University of Tsukuba, Tsukuba Science City, Ibaraki, Japan.

出版信息

FEBS Lett. 1999 Jan 15;442(2-3):221-5. doi: 10.1016/s0014-5793(98)01646-9.

Abstract

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.

摘要

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