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Vol. 11, Issue 12, 4403-4411, December 2000
and
Department of Biological Sciences, Laboratory for Molecular
Biology, University of Illinois at Chicago, Chicago, Illinois 60607
In yeast, the Ypt1 GTPase is required for
ER-to-cis-Golgi and cis-to-medial-Golgi
protein transport, while Ypt31/32 are a functional pair of GTPases
essential for exit from the trans-Golgi. We have previously identified
a Ypt1 guanine nucleotide exchange factor (GEF) activity and
characterized it as a large membrane-associated protein complex that
localizes to the Golgi and can be extracted from the membrane by salt,
but not by detergent. TRAPP is a large protein complex that is required
for ER-to-Golgi transport and that has properties similar to those of
Ypt1 GEF. Here we show that TRAPP has Ypt1 GEF activity.
GST-tagged Bet3p or Bet5p, two of the TRAPP subunits, were expressed in
yeast cells and were precipitated by glutathione-agarose (GA) beads.
The resulting precipitates can stimulate both GDP release and GTP
uptake by Ypt1p. The majority of the Ypt1 GEF activity associated with
the GST-Bet3p precipitate has an apparent molecular weight of > 670 kDa, indicating that the GEF activity resides in the TRAPP complex. Surprisingly, TRAPP can also stimulate nucleotide exchange on the
Ypt31/32 GTPases, but not on Sec4p, a Ypt-family GTPase required for
the last step of the exocytic pathway. Like the previously characterized Ypt1 GEF, the TRAPP Ypt1-GEF activity can be inhibited by
the nucleotide-free Ypt1-D124N mutant protein. This mutant protein also
inhibits the Ypt32 GEF activity of TRAPP. Coprecipitation and
overexpression studies suggest that TRAPP can act as a GEF for Ypt1 and
Ypt31/32 in vivo. These data suggest the exciting possibility that a
GEF complex common to Ypt1 and Ypt31/32 might coordinate the function
of these GTPases in entry into and exit from the Golgi.
Current address: Washington University School of
Medicine, Department of Pediatrics, St. Louis, MO.
Corresponding author. E-mail address:
nava{at}uic.edu.
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