ArticleEukaryotic cell2007
Use of bimolecular fluorescence complementation to study in vivo interactions between Cdc42p and Rdi1p of Saccharomyces cerevisiae.
Article in Eukaryotic cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 43 citations in OpenAlex.
- DLK orchestrates a modular transcriptional response to axon injury with separate roles for Fos and Jun.PLoS genetics · 2025Article
- Cdc42 GTPase-activating proteins (GAPs) regulate generational inheritance of cell polarity and cell shape in fission yeast.Molecular biology of the cell · 2021Article
- Establishment of tetracycline-regulated bimolecular fluorescence complementation assay to detect protein-protein interactions in Candida albicans.Scientific reports · 2020Article
- Applying bimolecular fluorescence complementation to screen and purify aquaporin protein:protein complexes.Protein science : a publication of the Protein Society · 2016Article
- Bimolecular Fluorescence Complementation (BiFC) Analysis: Advances and Recent Applications for Genome-Wide Interaction Studies.Journal of molecular biology · 2015Review
- Genome-wide bimolecular fluorescence complementation analysis of SUMO interactome in yeast.Genome research · 2013Article
- Vesicle trafficking from a lipid perspective: Lipid regulation of exocytosis in Saccharomyces cerevisiae.Cellular logistics · 2012Article
- Diversity in genetic in vivo methods for protein-protein interaction studies: from the yeast two-hybrid system to the mammalian split-luciferase system.Microbiology and molecular biology reviews : MMBR · 2012Review
- Sec1p and Mso1p C-terminal tails cooperate with the SNAREs and Sec4p in polarized exocytosis.Molecular biology of the cell · 2011Article
- WAVE forms hetero- and homo-oligomeric complexes at integrin junctions in Drosophila visualized by bimolecular fluorescence complementation.The Journal of biological chemistry · 2010Article
- Article
- The Rsr1/Bud1 GTPase interacts with itself and the Cdc42 GTPase during bud-site selection and polarity establishment in budding yeast.Molecular biology of the cell · 2010Article
- Mso1p regulates membrane fusion through interactions with the putative N-peptide-binding area in Sec1p domain 1.Molecular biology of the cell · 2010Article
- Inhibition of HIV-1 integrase nuclear import and replication by a peptide bearing integrase putative nuclear localization signal.Retrovirology · 2009Article
- Dual modes of cdc42 recycling fine-tune polarized morphogenesis.Developmental cell · 2009Article
- Visualization of molecular interactions using bimolecular fluorescence complementation analysis: characteristics of protein fragment complementation.Chemical Society reviews · 2009Review
- Energetic determinants of protein binding specificity: insights into protein interaction networks.Proteomics · 2009Article
- MCM-GINS and MCM-MCM interactions in vivo visualised by bimolecular fluorescence complementation in fission yeast.BMC cell biology · 2009Article
- The Rho GDI Rdi1 regulates Rho GTPases by distinct mechanisms.Molecular biology of the cell · 2008Article
- Molecular and functional characterization of a Rho GDP dissociation inhibitor in the filamentous fungus Tuber borchii.BMC microbiology · 2008Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Saccharomyces cerevisiae Cdc42p functions as a GTPase molecular switch, activating multiple signaling pathways required to regulate cell cycle progression and the actin cytoskeleton. Regulatory proteins control its GTP binding and hydrolysis and its subcellular localization, ensuring that Cdc42p is appropriately activated and localized at sites of polarized growth during the cell cycle. One of these, the Rdi1p guanine nucleotide dissociation inhibitor, negatively regulates Cdc42p by extracting it from cellular membranes. In this study, the technique of bimolecular fluorescence complementation (BiFC) was used to study the dynamic in vivo interactions between Cdc42p and Rdi1p. The BiFC data indicated that Cdc42p and Rdi1p interacted in the cytoplasm and around the periphery of the cell at the plasma membrane and that this interaction was enhanced at sites of polarized cell growth during the cell cycle, i.e., incipient bud sites, tips and sides of small- and medium-sized buds, and the mother-bud neck region. In addition, a ring-like structure containing the Cdc42p-Rdi1p complex transiently appeared following release from G1-phase cell cycle arrest. A homology model of the Cdc42p-Rdi1p complex was used to introduce mutations that were predicted to affect complex formation. These mutations resulted in altered BiFC interactions, restricting the complex exclusively to either the plasma membrane or the cytoplasm. Data from these studies have facilitated the temporal and spatial modeling of Rdi1p-dependent extraction of Cdc42p from the plasma membrane during the cell cycle.
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