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Vol. 11, Issue 3, 807-817, March 2000
and¶
*Friedrich-Miescher Laboratorium der Max-Planck-Gesellschaft, 72076 Tübingen, Germany; Yeast vacuoles undergo cycles of fragmentation and fusion as part
of their transmission to the daughter cell and in response to changes
of nutrients and the environment. Vacuole fusion can be reconstituted
in a cell free system. We now show that the vacuoles synthesize
phosphoinositides during in vitro fusion. Of these phosphoinositides,
phosphatidylinositol 4-phosphate and
phosphatidylinositol 4,5-bisphosphate
(PI(4,5)P2) are important for fusion. Monoclonal antibodies
to PI(4,5)P2, neomycin (a phosphoinositide ligand), and
phosphatidylinositol-specific phospholipase C interfere with the reaction. Readdition of PI(4,5)P2 restores fusion in
each case. Phosphatidylinositol 3-phosphate and
PI(3,5)P2 synthesis are not required. PI(4,5)P2
is necessary for priming, i.e., for the Sec18p (NSF)-driven
release of Sec17p (Department of Biochemistry,
Dartmouth Medical School, Hanover, New Hampshire 03755-3844;
§Institut für Biochemie II, 07740 Jena, Germany;
¶Lehrstuhl für Mikrobiologie, Biozentrum der
Universität, Am Hubland, 97074 Würzburg, Germany; and
Department of Anatomy, Medical School, Birmingham
B15-2TT, United Kingdom
-SNAP), which activates the vacuoles for
subsequent tethering and docking. Therefore, it represents the
kinetically earliest requirement identified for vacuole fusion so far.
Furthermore, PI(4,5)P2 is required at a step that can only
occur after docking but before the BAPTA sensitive step in the latest
stage of the reaction. We hence propose that PI(4,5)P2
controls two steps of vacuole fusion.
Corresponding author. E-mail
address: Andreas.Mayer{at}Tuebingen.mpg.de.
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