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

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 bo...

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Bibliographic Details
Published in:The Journal of biological chemistry 2005-10, Vol.280 (41), p.34489-34499
Main Authors: Lay, Dorothee, Grosshans, Bianka L., Heid, Hans, Gorgas, Karin, Just, Wilhelm W.
Format: Article
Language:English
Subjects:
Adenosine Triphosphate - chemistry
Adenosine Triphosphate - metabolism
ADP-Ribosylation Factor 1 - metabolism
ADP-Ribosylation Factors - chemistry
ADP-Ribosylation Factors - metabolism
ADP-Ribosylation Factors - physiology
Amino Acid Sequence
Animals
Brefeldin A - pharmacology
Cell Proliferation
Cytosol - metabolism
Genotype
Golgi Apparatus - metabolism
Guanosine Triphosphate - metabolism
Hydrolysis
In Vitro Techniques
Lipids - chemistry
Liver - metabolism
Mass Spectrometry
Molecular Sequence Data
Mutation
Oleic Acid - chemistry
Peroxisomes - metabolism
Protein Binding
Rats
Saccharomyces cerevisiae
Saccharomyces cerevisiae - metabolism
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
Subcellular Fractions
Trypsin - pharmacology
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M503497200