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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Bibliographic Details
Published in:Science (American Association for the Advancement of Science) 2001-05, Vol.292 (5520), p.1376-1378
Main Authors: Kang, Pil Jung, Sanson, Anthony, Lee, Bongyong, Park, Hay-Oak
Format: Article
Language:English
Subjects:
Art and archaeology
Ax12 protein
Biochemistry
Bud10 protein
Bud3 protein
Bud8 protein
Bud9 protein
Budding
Cell Division
Cell Polarity
Cell research
Cells
Cytological research
Cytoskeleton
Daughter cells
Daughters
Diploidy
Fungal Proteins - genetics
Fungal Proteins - metabolism
Genes, Fungal - genetics
Genotype
Geodetic position
guanine nucleotide exchange factor
Guanine Nucleotide Exchange Factors
Guanosine Diphosphate - metabolism
Guanosine Triphosphate - metabolism
Haploidy
Landmarks
Membrane Glycoproteins - genetics
Membrane Glycoproteins - metabolism
Mother cells
Mothers
Mutation - genetics
Plasmids
Precipitin Tests
Protein Binding
Recombinant Fusion Proteins - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins
Site Selection
Yeasts
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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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.1060360