ArticleMolecular biology of the cell2007
Identification of novel membrane-binding domains in multiple yeast Cdc42 effectors.
Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 65 citations in OpenAlex.
- Cdc42-Specific GTPase-Activating Protein Rga1 Squelches Crosstalk between the High-Osmolarity Glycerol (HOG) and Mating Pheromone Response MAPK Pathways.Biomolecules · 2021Article
- Stress-Activated Protein Kinase Signalling Regulates Mycoparasitic Hyphal-Hyphal Interactions inJournal of fungi (Basel, Switzerland) · 2021Article
- Role of Phosphatidylethanolamine Biosynthesis in Herpes Simplex Virus 1-Infected Cells in Progeny Virus Morphogenesis in the Cytoplasm and in Viral PathogenicityJournal of virology · 2020Article
- Regulation of intrinsic polarity establishment by a differentiation-type MAPK pathway inJournal of cell science · 2020Article
- Cell-cycle control of cell polarity in yeast.The Journal of cell biology · 2019Article
- The shared role of the Rsr1 GTPase and Gic1/Gic2 in Cdc42 polarization.Molecular biology of the cell · 2018Article
- Local and global Cdc42 guanine nucleotide exchange factors for fission yeast cell polarity are coordinated by microtubules and the Tea1-Tea4-Pom1 axis.Journal of cell science · 2018Article
- Article
- Importance of the REM (Ras exchange) domain for membrane interactions by RasGRP3.Biochimica et biophysica acta. Biomembranes · 2017Article
- Spatial regulation of organelle release from myosin V transport by p21-activated kinases.The Journal of cell biology · 2017Article
- Multiple Roles of the Cytoplasmic Domain of Herpes Simplex Virus 1 Envelope Glycoprotein D in Infected Cells.Journal of virology · 2016Article
- Heterotrimeric G Protein-coupled Receptor Signaling in Yeast Mating Pheromone Response.The Journal of biological chemistry · 2016Review
- PAK6 targets to cell-cell adhesions through its N-terminus in a Cdc42-dependent manner to drive epithelial colony escape.Journal of cell science · 2016Article
- Bem3, a Cdc42 GTPase-activating protein, traffics to an intracellular compartment and recruits the secretory Rab GTPase Sec4 to endomembranes.Journal of cell science · 2013Article
- Synergistic activation of p21-activated kinase 1 by phosphatidylinositol 4,5-bisphosphate and Rho GTPases.The Journal of biological chemistry · 2013Article
- Cdc42p regulation of the yeast formin Bni1p mediated by the effector Gic2p.Molecular biology of the cell · 2012Article
- A steep phosphoinositide bis-phosphate gradient forms during fungal filamentous growth.The Journal of cell biology · 2012Article
- Cell polarization and cytokinesis in budding yeast.Genetics · 2012Review
- A systems biology analysis of long and short-term memories of osmotic stress adaptation in fungi.BMC research notes · 2012Article
- A framework for mapping, visualisation and automatic model creation of signal-transduction networks.Molecular systems biology · 2012Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The Rho-type GTPase Cdc42 is a central regulator of eukaryotic cell polarity and signal transduction. In budding yeast, Cdc42 regulates polarity and mitogen-activated protein (MAP) kinase signaling in part through the PAK-family kinase Ste20. Activation of Ste20 requires a Cdc42/Rac interactive binding (CRIB) domain, which mediates its recruitment to membrane-associated Cdc42. Here, we identify a separate domain in Ste20 that interacts directly with membrane phospholipids and is critical for its function. This short region, termed the basic-rich (BR) domain, can target green fluorescent protein to the plasma membrane in vivo and binds PIP(2)-containing liposomes in vitro. Mutation of basic or hydrophobic residues in the BR domain abolishes polarized localization of Ste20 and its function in both MAP kinase-dependent and independent pathways. Thus, Cdc42 binding is required but is insufficient; instead, direct membrane binding by Ste20 is also required. Nevertheless, phospholipid specificity is not essential in vivo, because the BR domain can be replaced with several heterologous lipid-binding domains of varying lipid preferences. We also identify functionally important BR domains in two other yeast Cdc42 effectors, Gic1 and Gic2, suggesting that cooperation between protein-protein and protein-membrane interactions is a prevalent mechanism during Cdc42-regulated signaling and perhaps for other dynamic localization events at the cell cortex.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.