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J. Biol. Chem., Vol. 280, Issue 41, 34489-34499, October 14, 2005

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Binding and Functions of ADP-ribosylation Factor on Mammalian and Yeast Peroxisomes^*

Dorothee Lay, Bianka L. Grosshans, Hans Heid¶, Karin Gorgas||, and Wilhelm W. Just1

From the Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany, the Department of Cell Biology, Yale University, New Haven, Connecticut 06520, the ^¶Deutsches Krebsforschungszentrum Heidelberg, D-69120 Heidelberg, Germany, and the ^||Institut für Anatomie und Zellbiologie, Universität Heidelberg, D-69120 Heidelberg, Germany

We have analyzed in vitro the binding characteristics of members of the ADP-ribosylation factor (ARF) family of proteins to a highly purified rat liver peroxisome preparation void of Golgi membranes and studied in vivo a role these proteins play in the proliferation of yeast peroxisomes. Although both ARF1 and ARF6 were found on peroxisomes, coatomer recruitment only depended on ARF1-GTP. Recruitment of ARF1 and coatomer to peroxisomes was significantly affected both by pretreating the animals with peroxisome proliferators and by ATP and a cytosolic fraction designated the intermediate pool fraction depleted of ARF and coatomer. In the presence of ATP, the concentrations of ARF1 and coatomer on peroxisomes were reduced, whereas intermediate pool fraction led to a concentration-dependent decrease in ARF and increase in coatomer. Brefeldin A, a fungal toxin that is known to reduce ARF1 binding to Golgi membranes, did not affect ARF1 binding to peroxisomes. In Saccharomyces cerevisiae, both ScARF1 and ScARF3, the yeast orthologs of mammalian ARF1 and ARF6, were implicated in the control of peroxisome proliferation. ScARF1 regulated this process in a positive manner, and ScARF3 regulated it in a negative manner.

Received for publication, March 30, 2005 , and in revised form, August 5, 2005.

^* This work was supported by the FP6 European Union Project "Peroxisome" (LSHG-CT-2004-512018) and Deutsche Forschungsgemeinschaft Grant SFB 638. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, Heidelberg D-69120, Germany. Tel.: 49-6221-544155; Fax: 49-6221-544366; E-mail: wilhelm.just{at}urz.uni-heidelberg.de.

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