A GDP/GTP Exchange Factor Involved in Linking a Spatial Landmark to Cell Polarity

In both animal and yeast cells, signaling pathways involving small guanosine triphosphatases (GTPases) regulate polarized organization of the actin cytoskeleton. In the budding yeast Saccharomyces cerevisiae, the Ras-like GTPase Bud1/Rsr1 and its guanosine 5′-diphosphate (GDP)/guanosine 5′-triphosph...

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Published inScience (American Association for the Advancement of Science) Vol. 292; no. 5520; pp. 1376 - 1378
Main Authors Kang, Pil Jung, Sanson, Anthony, Lee, Bongyong, Park, Hay-Oak
Format Journal Article
LanguageEnglish
Published Washington, DC American Society for the Advancement of Science 18.05.2001
American Association for the Advancement of Science
The American Association for the Advancement of Science
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Summary:In both animal and yeast cells, signaling pathways involving small guanosine triphosphatases (GTPases) regulate polarized organization of the actin cytoskeleton. In the budding yeast Saccharomyces cerevisiae, the Ras-like GTPase Bud1/Rsr1 and its guanosine 5′-diphosphate (GDP)/guanosine 5′-triphosphate (GTP) exchange factor Bud5 are involved in the selection of a specific site for growth, thus determining cell polarity. We found that Bud5 is localized at the cell division site and the presumptive bud site. Its localization is dependent on potential cellular landmarks, such as Bud3 and Axl2/Bud10 in haploid cells and Bud8 and Bud9 in diploid cells. Bud5 also physically interacts with Axl2/Bud10, a transmembrane glycoprotein, suggesting that a receptor-like transmembrane protein recruits a GDP/GTP exchange factor to connect an intrinsic spatial signal to oriented cell growth.
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ISSN:0036-8075
1095-9203
DOI:10.1126/science.1060360