title: Binding and functions of ADP-ribosylation factor on mammalian and yeast peroxisomes.
abstract: 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.
authors.affiliation: Biochemie-Zentrum der Universität Heidelberg, Im Neuenheimer Feld 328, D-69120 Heidelberg, Germany.
authors.forename: Dorothee
authors.initials: D
authors.lastname: Lay
authors.forename: Bianka
authors.initials: B
authors.lastname: L Grosshans
authors.forename: Hans
authors.initials: H
authors.lastname: Heid
authors.forename: Karin
authors.initials: K
authors.lastname: Gorgas
authors.forename: Wilhelm W
authors.initials: WW
authors.lastname: Just
mesh_terms: D020823:ADP-Ribosylation Factor 1 / Q000378:metabolism; D000089982:ADP-Ribosylation Factor 6; D020727:ADP-Ribosylation Factors / Q000737:chemistry / Q000378:metabolism / Q000502:physiology*; D000255:Adenosine Triphosphate / Q000737:chemistry / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D020126:Brefeldin A / Q000494:pharmacology; D049109:Cell Proliferation; D003600:Cytosol / Q000378:metabolism; D005838:Genotype; D006056:Golgi Apparatus / Q000378:metabolism; D006160:Guanosine Triphosphate / Q000378:metabolism; D006868:Hydrolysis; D066298:In Vitro Techniques; D008055:Lipids / Q000737:chemistry; D008099:Liver / Q000378:metabolism; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009154:Mutation; D019301:Oleic Acid / Q000737:chemistry; D020675:Peroxisomes / Q000378:metabolism*; D011485:Protein Binding; D051381:Rats; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013347:Subcellular Fractions; D014357:Trypsin / Q000494:pharmacology
chemical_list: D000089982:ADP-Ribosylation Factor 6; D008055:Lipids; D020126:Brefeldin A; D019301:Oleic Acid; D006160:Guanosine Triphosphate; D000255:Adenosine Triphosphate; D014357:Trypsin; D020823:ADP-Ribosylation Factor 1; D020727:ADP-Ribosylation Factors; C000715349:Arf6 protein, rat