ArticleMolecular and cellular biology2000
Role of Cdc42p in pheromone-stimulated signal transduction in Saccharomyces cerevisiae.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
42 citing papers in PubMed, 79 citations in OpenAlex.
- Review
- Mechanisms and Virulence Factors ofJournal of fungi (Basel, Switzerland) · 2024Review
- Strain-dependent differences in coordination of yeast signalling networks.The FEBS journal · 2023Article
- Exploratory polarization facilitates mating partner selection inMolecular biology of the cell · 2021Article
- Crosstalk and spatiotemporal regulation between stress-induced MAP kinase pathways and pheromone signaling in budding yeast.Cell cycle (Georgetown, Tex.) · 2020Review
- Systematic analysis of F-box proteins reveals a new branch of the yeast mating pathway.The Journal of biological chemistry · 2019Article
- Cell-cycle control of cell polarity in yeast.The Journal of cell biology · 2019Article
- Sec14-nodulin proteins and the patterning of phosphoinositide landmarks for developmental control of membrane morphogenesis.Molecular biology of the cell · 2015Article
- Bud3 activates Cdc42 to establish a proper growth site in budding yeast.The Journal of cell biology · 2014Article
- Cellular noise suppression by the regulator of G protein signaling Sst2.Molecular cell · 2014Article
- A Cdc42- and Rac-interactive binding (CRIB) domain mediates functions of coronin.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Inhibition of Cdc42 during mitotic exit is required for cytokinesis.The Journal of cell biology · 2013Article
- Mate and fuse: how yeast cells do it.Open biology · 2013Review
- Cdc42p and Fus2p act together late in yeast cell fusion.Molecular biology of the cell · 2012Article
- Article
- The putative lipid transporter, Arv1, is required for activating pheromone-induced MAP kinase signaling in Saccharomyces cerevisiae.Genetics · 2011Article
- Symmetry breaking in the life cycle of the budding yeast.Cold Spring Harbor perspectives in biology · 2009Review
- Distinct roles for two Galpha-Gbeta interfaces in cell polarity control by a yeast heterotrimeric G protein.Molecular biology of the cell · 2008Article
- Identification of novel membrane-binding domains in multiple yeast Cdc42 effectors.Molecular biology of the cell · 2007Article
- Sequential and distinct roles of the cadherin domain-containing protein Axl2p in cell polarization in yeast cell cycle.Molecular biology of the cell · 2007Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
CDC42 encodes a highly conserved GTPase of the Rho family that is best known for its role in regulating cell polarity and actin organization. In addition, various studies of both yeast and mammalian cells have suggested that Cdc42p, through its interaction with p21-activated kinases (PAKs), plays a role in signaling pathways that regulate target gene transcription. However, recent studies of the yeast pheromone response pathway suggested that prior results with temperature-sensitive cdc42 mutants were misleading and that Cdc42p and the Cdc42p-PAK interaction are not involved in signaling. To clarify this issue, we have identified and characterized novel viable pheromone-resistant cdc42 alleles that retain the ability to perform polarity-related functions. Mutation of the Cdc42p residue Val36 or Tyr40 caused defects in pheromone signaling and in the localization of the Ste20p PAK in vivo and affected binding to the Ste20p Cdc42p-Rac interactive binding (CRIB) domain in vitro. Epistasis analysis suggested that they affect the signaling step at which Ste20p acts, and overproduction of Ste20p rescued the defect. These results suggest that Cdc42p is in fact required for pheromone response and that interaction with the PAK Ste20p is critical for that role. Furthermore, the ste20DeltaCRIB allele, previously used to disrupt the Cdc42p-Ste20p interaction, behaved as an activated allele, largely bypassing the signaling defect of the cdc42 mutants. Additional observations lead us to suggest that Cdc42p collaborates with the SH3-domain protein Bem1p to facilitate signal transduction, possibly by providing a cell surface scaffold that aids in the local concentration of signaling kinases, thus promoting activation of a mitogen-activated protein kinase cascade by Ste20p.
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Registered trials
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.