标题：Bacterial ADP-ribosyltransferase with a substrate specificity of the rho protein disassembles the Golgi apparatus in Vero cells and mimics the action of brefeldin A.
期刊名称：Proceedings of the National Academy of Sciences
印刷版ISSN：0027-8424
电子版ISSN：1091-6490
出版年度：1992
卷号：89
期号：19
页码：8903-8907
DOI：10.1073/pnas.89.19.8903
语种：English
出版社：The National Academy of Sciences of the United States of America
摘要：Epidermal-cell differentiation inhibitor (EDIN) is an exoenzyme produced by Staphylococcus aureus that catalyzes the ADP-ribosylation of rho proteins, members of the small GTP-binding protein family. In this study we demonstrate that EDIN induces a rapid morphological change in the Golgi structure of monkey kidney Vero cells that is similar to the changes elicited by brefeldin A (BFA). Treatment of Vero cells with EDIN resulted in a rapid disappearance of N-7-(4-nitrobenzo-2-oxa-1,3-diazole)-6-aminocaproylsphingosine, a 110-kDa protein (beta-COP, coat protein), and mannosidase II from the Golgi structure. Lower doses of EDIN and BFA had a synergistic effect on the redistribution of the Golgi markers. The similarities in the effects of EDIN and BFA in Vero cells also include the EDIN- or BFA-mediated protection of Vero cells from ricin cytotoxicity and prevention of the effects of EDIN or BFA on the distribution of Golgi markers by the pretreatment of Vero cells with guanosine 5'-[gamma-thio]triphosphate or forskolin. Incubation of a Vero-cell homogenate with [32P]NAD+ and EDIN in vitro resulted in the appearance of a labeled band with an apparent molecular mass of 22 kDa. The morphological change of the Golgi structure induced by EDIN was inhibited by nicotinamide, an inhibitor of EDIN-catalyzed ADP-ribosylation. Thus these data suggest that a rho protein is involved in the membrane trafficking between the Golgi and the endoplasmic reticulum of Vero cells and that this rho protein may be a target shared by EDIN and BFA.
