Published online May 12, 2008
doi:10.1083/jcb.200801101
The Journal of Cell Biology, Vol. 181, No. 4, 697-709
The Rockefeller University Press, 0021-9525 $30.00
© 2008 Paterson et al.
Dynamic localization of yeast Fus2p to an expanding ring at the cell fusion junction during mating
Joanna Mathis Paterson,
Casey A. Ydenberg, and
Mark D. Rose
Department of Molecular Biology, Princeton University, Princeton, NJ 08544
Correspondence to M.D. Rose: mdrose{at}princeton.edu
Fus2p is a pheromone-induced protein associated with the amphiphysin homologue Rvs161p, which is required for cell fusion during mating in Saccharomyces cerevisiae. We constructed a functional Fus2p–green fluorescent protein (GFP), which exhibits highly dynamic localization patterns in pheromone-responding cells (shmoos): diffuse nuclear, mobile cytoplasmic dots and stable cortical patches concentrated at the shmoo tip. In mitotic cells, Fus2p-GFP is nuclear but becomes cytoplasmic as cells form shmoos, dependent on the Fus3p protein kinase and high levels of pheromone signaling. The rapid cytoplasmic movement of Fus2p-GFP dots requires Rvs161p and polymerized actin and is aberrant in mutants with compromised actin organization, which suggests that the Fus2p dots are transported along actin cables, possibly in association with vesicles. Maintenance of Fus2p-GFP patches at the shmoo tip cortex is jointly dependent on actin and a membrane protein, Fus1p, which suggests that Fus1p is an anchor for Fus2p. In zygotes, Fus2p-GFP forms a dilating ring at the cell junction, returning to the nucleus at the completion of cell fusion.
Abbreviations used in this paper: GEF, guanine nucleotide exchange factor; IP, immunoprecipitation; lat-A, latrunculin-A; MAP, mitogen-activated protein; ZCF, zone of cell fusion.
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