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 p
otential to bind coatomer, Biochemical as well as immunocytochemical e
vidence is presented showing that peroxisomes incubated with preparati
ons of bovine brain or rat liver cytosol recruit ADP-ribosylation fact
or (ARF) and coatomer in a strictly guanosine 5'-O-(3-thiotriphosphate
)-dependent manner. Consistent with this observation, IdlF cells expre
ssing a temperature-sensitive mutant version of the epsilon-subunit of
coatomer exhibit elongated tubular peroxisomes possibly due to impair
ed vesiculation at the nonpermissive temperature. Since overexpression
of Pex11p in Chinese hamster ovary wild-type cells causes proliferati
on of peroxisomes, these data suggest that Pex11p plays an important r
ole in peroxisome biogenesis by supporting ARF-and coatomer-dependent
vesiculation of the organelles.