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J Biol Chem, Vol. 274, Issue 47, 33186-33189, November 19, 1999
tefan
Albert and
From the Max Planck Institute for Biophysical Chemistry, Department
of Molecular Genetics, D-37070 Göttingen, Germany
Monomeric GTPases of the Ras superfamily have a
very slow intrinsic GTPase activity which is accelerated by specific
GTPase-activating proteins. In contrast to Ras- and Rho-specific
GTPase-activating proteins (GAPs) that have been studied in great
detail, little is known about the functioning of GAPs specific for
Ypt/Rab transport GTPases. We have identified two novel Ypt/Rab-GAPs
because of their sequence relatedness to the three known GAPs Gyp1p,
Gyp6p, and Gyp7p. Mdr1/Gyp2p is an efficient GAP for Ypt6p and Sec4p, whereas Msb3/Gyp3p is a potent GAP for Sec4p, Ypt6p, Ypt51p,
Ypt31/Ypt32p, and Ypt1p. Although the affinity of Msb3/Gyp3p for its
preferred substrate Sec4p is low (Km = 154 µM), it accelerates the intrinsic GTPase activity of
Sec4p 5 × 105-fold. Msb3/Gyp3p appears to be
functionally linked to Cdc42p-regulated pathway(s). The results
demonstrate that in yeast there is a large family of Ypt/Rab-GAPs,
members of which discriminate poorly between GTPases involved in
regulating different steps of exo- and endocytic transport routes.
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