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J. Biol. Chem., Vol. 277, Issue 43, 41023-41031, October 25, 2002
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From the Max-Planck-Institute for Biophysical Chemistry, Department
of Molecular Genetics, D-37070 Göttingen, Germany
We here report on the identification and detailed
biochemical characterization of two novel GTPase-activating proteins,
Gyp5p and Gyp8p, whose efficient substrate is Ypt1p, a Ypt/Rab-GTPase essential for endoplasmic reticulum-to-Golgi trafficking in yeast. Gyp5p accelerated the intrinsic GTPase activity of Ypt1p 4.2 × 104-fold and, surprisingly, the 40-fold reduced GTP
hydrolysis rate of Ypt1(Q67L)p 1.5 × 104-fold. At
steady state, the two newly discovered GTPase-activating proteins
(GAPs) as well as the previously described Gyp1p, which also uses Ypt1p
as the preferred substrate, display different subcellular localization.
To add to an understanding of the significance of Ypt1p-bound GTP
hydrolysis in vivo, yeast strains expressing the
GTPase-deficient Ypt1(Q67L)p and having different Ypt1-GAP genes
deleted were created. Depending on the genetic background, different
mutants exhibited growth defects at low temperature and, already at
permissive temperature, various morphological alterations resembling
autophagy. Transport of proteins was not significantly impaired. Growth
defects of Ypt1(Q67L)-expressing cells could be suppressed on high
expression of all three Ypt1-GAPs. We propose that permanently active
Ypt1p leads to increased vesicle fusion, which might induce previously
unnoticed autophagic degradation of exaggerated membrane-enclosed
structures. The data indicate that hydrolysis of Ypt1p-bound GTP is a
prerequisite for a balanced vesicle flow between endoplasmic reticulum
and Golgi compartments.
Significance of GTP Hydrolysis in Ypt1p-regulated Endoplasmic
Reticulum to Golgi Transport Revealed by the Analysis of Two Novel
Ypt1-GAPs*
,
tefan
Albert¶
*
This work was supported by the Max Planck Society and by
grants from the Deutsche Forschungsgemeinschaft, the Human Frontier Science Program, and Fonds der Chemischen Industrie (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.
Present address: European Institute of Oncology, Dept. of
Experimental Oncology, Milan 20141, Italy.
§
To whom correspondence should be addressed. Tel.: 49-551-201-1496;
Fax: 49-551-201-1718; E-mail: dgallwi1@gwdg.de.
¶
Present address: Institute of Radiation and Cell Research,
Versbacher Str. 5, D-97078 Würzburg, Germany.
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