Interactions between the bud emergence proteins Bem1p and Bem2p and Rho-type GTPases in yeast.
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The SH3 domain-containing protein Bem1p is needed for normal bud emergence and mating projection formation, two processes that require asymmetric reorganizations of the cortical cytoskeleton in Saccharomyces cerevisiae. To identify proteins that functionally and/or physically interact with Bem1p, we screened for mutations that display synthetic lethality with a mutant allele of the BEM1 gene and for genes whose products display two-hybrid interactions with the Bem1 protein. CDC24, which is required for bud emergence and encodes a GEF (guanine-nucleotide exchange factor) for the essential Rho-type GTPase Cdc42p, was identified during both screens. The COOH-terminal 75 amino acids of Cdc24p, outside of the GEF domain, can interact with a portion of Bem1p that lacks both SH3 domains. Bacterially expressed Cdc24p and Bem1p bind to each other in vitro, indicating that no other yeast proteins are required for this interaction. The most frequently identified gene that arose from the bem1 synthetic-lethal screen was the bud-emergence gene BEM2 (Bender and Pringle. 1991. Mol. Cell Biol. 11:1295-1395), which is allelic with IPL2 (increase in ploidy; Chan and Botstein, 1993. Genetics. 135:677-691). Here we show that Bem2p contains a GAP (GTPase-activating protein) domain for Rho-type GTPases, and that this portion of Bem2p can stimulate in vitro the GTPase activity of Rho1p, a second essential yeast Rho-type GTPase. Cells deleted for BEM2 become large and multinucleate. These and other genetic, two-hybrid, biochemical, and phenotypic data suggest that multiple Rho-type GTPases control the reorganization of the cortical cytoskeleton in yeast and that the functions of these GTPases are tightly coupled. Also, these findings raise the possibility that Bem1p may regulate or be a target of action of one or more of these GTPases.
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CgBem2 functions as a GAP for CgRho1.
“The morphology defects and presence of higher amounts of active (GTP-bound) Rho GTPase and of phosphorylated CgSlt2 in mutants lacking CgBEM2 suggest that CgBem2 functions as a GAP for CgRho1, consistent with its known role in S. cerevisiae (53).”
From The Rho1 GTPase-activating protein CgBem2 is required for survival of azole stress in Candida glabrata (2011) · cites this paper as [53]
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- Authors
- Peterson, J., Zheng, Y., Bender, L., Myers, A., Cerione, R., & Bender, A.
- Affiliations
- Indiana University Bloomington (US)
- Venue
- The Journal of cell biology
- Publisher
- Rockefeller University Press
- Published
- 1994-12-01
- Volume
- 127
- Issue
- 5
- Pages
- 1395-1406
- ISSN
- 0021-9525 (ISSN-L)
- 1540-8140
- PMC
- PMC2120249
- OpenAlex
- W2125781144
- Cited by
- 197
- References
- 60
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 2 · 2023: 3 · 2022: 2 · 2021: 2 · 2020: 6 · 2019: 4 · 2018: 2 · 2017: 3 · 2016: 1 · 2015: 4 · 2014: 3 · 2013: 5 · 2012: 5
- FWCI
- 5.82
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Licence
- cc-by-nc-sa
- Locations
- The Journal of Cell Biology (publishedVersion)
- PubMed Central (publishedVersion, cc-by-nc-sa)
- PubMed (publishedVersion)
- Funders
- National Institute of General Medical Sciences (GM 47458, R01GM047458, GM46271)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
- Keywords
- Cdc42p, Rho1p, bud emergence, Cdc24, guanine nucleotide exchange factor, GTPase-activating protein, SH3 domain, protein-protein interaction, synthetic lethality, multinucleated cells, Saccharomyces cerevisiae
- MeSH terms
- Amino Acid Sequence, Base Sequence, Cloning, Molecular, Fungal Proteins, Genes, Fungal, Genes, Lethal, Molecular Sequence Data, Morphogenesis, Mutation, Proto-Oncogene Proteins, Saccharomyces cerevisiae, Cell Cycle Proteins, GTP-Binding Proteins, GTP Phosphohydrolases, Guanine Nucleotide Exchange Factors, GTPase-Activating Proteins, rho GTP-Binding Proteins, Saccharomyces cerevisiae Proteins, Adaptor Proteins, Signal Transducing
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