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J. Biol. Chem., Vol. 278, Issue 2, 791-799, January 10, 2003
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From the Max Planck Institute for Biophysical Chemistry, Department
of Molecular Genetics, D-37070 Göttingen, Germany
Yeast Ypt6p, the homologue of the mammalian Rab6
GTPase, is not essential for cell viability. Based on previous studies
with ypt6 deletion mutants, a regulatory role of the GTPase
either in protein retrieval to the trans-Golgi network or
in forward transport between the endoplasmic reticulum (ER) and early
Golgi compartments was proposed. To assess better the primary role(s) of Ypt6p, temperature-sensitive ypt6 mutants were generated
and analyzed biochemically and genetically. Defects in
N-glycosylation of proteins passing the Golgi and of
Golgi-resident glycosyltransferases as well as protein sorting defects
in the trans-Golgi were recorded shortly after functional
loss of Ypt6p. ER-to-Golgi transport and protein secretion were delayed
but not interrupted. Mis-sorting of the vesicular SNARE Sec22p
to the late Golgi was also observed. Combination of the
ypt6-2 mutant allele with a number of mutants in forward
and retrograde transport between ER, Golgi, and endosomes led to
synthetic negative growth defects. The results obtained indicate that
Ypt6p acts in endosome-to-Golgi, in intra-Golgi retrograde
transport, and possibly also in Golgi-to-ER trafficking.
Biochemical and Genetic Evidence for the Involvement of Yeast
Ypt6-GTPase in Protein Retrieval to Different Golgi Compartments*
*
This work was supported by the Max Planck Society and by
grants from the Deutsche Forschungsgemeinschaft, the Fonds der
Chemischen Industrie, and the Human Frontier Science Program (to
D. G.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed. Tel.: 49-551-201-1496;
Fax: 49-551-201-1718; E-mail: Dieter.Gallwitz@mpi-bpc.mpg.de.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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