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

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