ArticleMolecular and cellular biology1993
Influence of guanine nucleotides on complex formation between Ras and CDC25 proteins.
Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed, 147 citations in OpenAlex.
- Genetic and oncogenic features of RASGRF fusions.NPJ precision oncology · 2025Article
- Pathogen-specific structural features ofmBio · 2023Article
- The Cdc25 and Ras1 Proteins ofJournal of fungi (Basel, Switzerland) · 2023Article
- Beyond IgE: Alternative Mast Cell Activation Across Different Disease States.International journal of molecular sciences · 2020Review
- Mapping the proximity interaction network of the Rho-family GTPases reveals signalling pathways and regulatory mechanisms.Nature cell biology · 2020Article
- SH3-class Ras guanine nucleotide exchange factors are essential for Aspergillus fumigatus invasive growth.Cellular microbiology · 2019Article
- Reconstruction of thermotolerant yeast by one-point mutation identified through whole-genome analyses of adaptively-evolved strains.Scientific reports · 2016Article
- Recurrent mTORC1-activating RRAGC mutations in follicular lymphoma.Nature genetics · 2016Article
- Inside-Out Signaling Pathways from Nuclear Reactive Oxygen Species Control Pulmonary Innate Immunity.Journal of innate immunity · 2016Review
- The Potential Role of 8-Oxoguanine DNA Glycosylase-Driven DNA Base Excision Repair in Exercise-Induced Asthma.Mediators of inflammation · 2016Review
- Systematic identification of cell size regulators in budding yeast.Molecular systems biology · 2014Article
- The role of 8-oxoguanine DNA glycosylase-1 in inflammation.International journal of molecular sciences · 2014Review
- Activation of ras signaling pathway by 8-oxoguanine DNA glycosylase bound to its excision product, 8-oxoguanine.The Journal of biological chemistry · 2012Article
- Article
- Regulation of macroautophagy in Saccharomyces cerevisiae.Seminars in cell & developmental biology · 2010Review
- EspM2 is a RhoA guanine nucleotide exchange factor.Cellular microbiology · 2010Article
- Real-time NMR study of guanine nucleotide exchange and activation of RhoA by PDZ-RhoGEF.The Journal of biological chemistry · 2010Article
- Deterministic mathematical models of the cAMP pathway in Saccharomyces cerevisiae.BMC systems biology · 2009Article
- Signal transduction at point-blank range: analysis of a spatial coupling mechanism for pathway crosstalk.Biophysical journal · 2008Article
- A novel Dictyostelium RasGEF required for chemotaxis and development.BMC cell biology · 2005Article
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The Saccharomyces cerevisiae CDC25 gene and closely homologous genes in other eukaryotes encode guanine nucleotide exchange factors for Ras proteins. We have determined the minimal region of the budding yeast CDC25 gene capable of activity in vivo. The region required for full biological activity is approximately 450 residues and contains two segments homologous to other proteins: one found in both Ras-specific exchange factors and the more distant Bud5 and Lte1 proteins, and a smaller segment of 48 amino acids found only in the Ras-specific exchange factors. When expressed in Escherichia coli as a fusion protein, this region of CDC25 was found to be a potent catalyst of GDP-GTP exchange on yeast Ras2 as well as human p21H-ras but inactive in promoting exchange on the Ras-related proteins Ypt1 and Rsr1. The CDC25 fusion protein catalyzed replacement of GDP-bound to Ras2 with GTP (activation) more efficiently than that of the reverse reaction of replacement of GTP for GDP (deactivation), consistent with prior genetic analysis of CDC25 which indicated a positive role in the activation of Ras. To more directly study the physical interaction of CDC25 and Ras proteins, we developed a protein-protein binding assay. We determined that CDC25 binds tightly to Ras2 protein only in the absence of guanine nucleotides. This higher affinity of CDC25 for the nucleotide-free form than for either the GDP- or GTP-bound form suggests that CDC25 catalyzes exchange of guanine nucleotides bound to Ras proteins by stabilization of the transitory nucleotide-free state.
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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.