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J. Cell Biol., Volume 141, Number 2, April 20, 1998 373-383

Peroxisome Biogenesis: Involvement of ARF and Coatomer

Michael Passreiter,* Markus Anton,* Dorothee Lay,* Rainer Frank,Dagger Cordula Harter,* Felix T. Wieland,* Karin Gorgas,§ and Wilhelm W. Just*

* Biochemie-Zentrum, Dagger  Zentrum für Molekülare Biologie Heidelberg, and § Institut für Anatomie und Zellbiologie II, Universität Heidelberg, D-69120 Heidelberg, Germany

Peroxisomal membrane protein (Pmp)26p (RnPex11p), a major constituent of induced rat liver peroxisomal membrane, was found to contain a COOH-terminal, cytoplasmically exposed consensus dilysine motif with the potential to bind coatomer. Biochemical as well as immunocytochemical evidence is presented showing that peroxisomes incubated with preparations of bovine brain or rat liver cytosol recruit ADP-ribosylation factor (ARF) and coatomer in a strictly guanosine 5'-O-(3-thiotriphosphate)-dependent manner. Consistent with this observation, ldlF cells expressing a temperature-sensitive mutant version of the epsilon -subunit of coatomer exhibit elongated tubular peroxisomes possibly due to impaired vesiculation at the nonpermissive temperature. Since overexpression of Pex11p in Chinese hamster ovary wild-type cells causes proliferation of peroxisomes, these data suggest that Pex11p plays an important role in peroxisome biogenesis by supporting ARF- and coatomer-dependent vesiculation of the organelles.


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