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Vol. 13, No. 17, pp. 2284-2300, September 1, 1999
1 Swiss Institute for Experimental Cancer Research (ISREC),
1066 Epalinges/VD, Switzerland; 2 Vienna
Biocenter, Institute of Biochemistry and Molecular Cell Biology,
University of Vienna and Ludwig Boltzmann-Forschungsstelle für
Biochemie, 1030 Vienna, Austria; 3 Department of Biochemistry
and Biophysics, University of California, San
Francisco, San Francisco, California 94143-0448 USA
Far1p is a bifunctional protein that is required to arrest the cell
cycle and to establish cell polarity during yeast mating. Far1p is
localized predominantly in the nucleus but accumulates in the cytoplasm
in cells exposed to pheromones. Here we show that Far1p functions in
both subcellular compartments: nuclear Far1p is required to arrest the
cell cycle, whereas cytoplasmic Far1p is involved in the establishment
of cell polarity. The subcellular localization of Far1p is regulated by
two mechanisms: (1) Far1p contains a functional bipartite nuclear
localization signal (NLS), and (2) Far1p is exported from the nucleus
by Msn5p/Ste21p, a member of the exportin family. Cells
deleted for Msn5p/Ste21p failed to export Far1p in
response to pheromones, whereas overexpression of
Msn5p/Ste21p was sufficient to accumulate Far1p in the
cytoplasm in the absence of pheromones. Msn5p/Ste21p was
localized in the nucleus and interacted with Far1p in a manner
dependent on GTP-bound Gsp1p. Two-hybrid analysis identified a small
fragment within Far1p that is necessary and sufficient for binding to
Msn5p/Ste21p, and is also required to export Far1p in
vivo. Finally, similar to 
msn5/ste21 strains,
cells expressing a mutant Far1p, which can no longer be exported,
exhibit a mating defect, but are able to arrest their cell cycle in
response to pheromones. Taken together, our results suggest that
nuclear export of Far1p by Msn5p/Ste21p coordinates the
two separable functions of Far1p during mating.
[Key Words: Export; cell cycle; mating; Msn5p/Ste21p; NLS]
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