Title: | Dynamic localization of yeast Fus2p to an expanding ring at the cell fusion junction during mating |
Author(s): | Paterson JM; Ydenberg CA; Rose MD; |
Address: | "Department of Molecular Biology, Princeton University, Princeton, NJ 08544, USA" |
ISSN/ISBN: | 1540-8140 (Electronic) 0021-9525 (Print) 0021-9525 (Linking) |
Abstract: | "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" |
Keywords: | "Actins/metabolism Bridged Bicyclo Compounds, Heterocyclic/pharmacology Cell Nucleus/drug effects/metabolism Cell Polarity/drug effects Cytoskeletal Proteins/*metabolism Green Fluorescent Proteins/metabolism Intercellular Junctions/drug effects/*metabolism;" |
Notes: | "MedlinePaterson, Joanna Mathis Ydenberg, Casey A Rose, Mark D eng R01 GM037739/GM/NIGMS NIH HHS/ R01 GM37739/GM/NIGMS NIH HHS/ Research Support, N.I.H., Extramural 2008/05/14 J Cell Biol. 2008 May 19; 181(4):697-709. doi: 10.1083/jcb.200801101. Epub 2008 May 12" |