ArticleNature communications2017
p190RhoGAP proteins contain pseudoGTPase domains.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed, 24 citations in OpenAlex.
- Structural basis of pseudoGTPase-mediated protein-protein interactions.Structure (London, England : 1993) · 2025Article
- Using integrative bioinformatics approaches and machine-learning strategies to identify potential signatures for atrial fibrillation.International journal of cardiology. Heart & vasculature · 2025Article
- TMEM16A partners with mTOR to influence pathways of cell survival, proliferation, and migration in cholangiocarcinoma.American journal of physiology. Gastrointestinal and liver physiology · 2023Article
- Emerging functions of pseudoenzymes.The Biochemical journal · 2023Review
- Structure Determination of SH2-Phosphopeptide Complexes by X-Ray Crystallography: The Example of p120RasGAP.Methods in molecular biology (Clifton, N.J.) · 2023Article
- DUSP5P1 promotes gastric cancer metastasis and platinum drug resistance.Oncogenesis · 2022Article
- The Hippo pathway mediates Semaphorin signaling.Science advances · 2022Article
- Fixing the GAP: The role of RhoGAPs in cancer.European journal of cell biology · 2022Review
- Mechanoregulation of Vascular Endothelial Growth Factor Receptor 2 in Angiogenesis.Frontiers in cardiovascular medicine · 2021Review
- The pseudoGTPase group of pseudoenzymes.The FEBS journal · 2020Review
- Review
- Investigation of the role and mechanism of ARHGAP5-mediated colorectal cancer metastasis.Theranostics · 2020Article
- p190RhoGAPs, theCells · 2019Review
- Crystal structures of p120RasGAP N-terminal SH2 domain in its apo form and in complex with a p190RhoGAP phosphotyrosine peptide.PloS one · 2019Article
- PseudoGTPase domains in p190RhoGAP proteins: a mini-review.Biochemical Society transactions · 2018Review
- The N-Terminal GTPase Domain of p190RhoGAP Proteins Is a PseudoGTPase.Structure (London, England : 1993) · 2018Article
- The crystal structure of pseudokinase PEAK1 (Sugen kinase 269) reveals an unusual catalytic cleft and a novel mode of kinase fold dimerization.The Journal of biological chemistry · 2018Article
- MicroRNAs as Potential Targets for Therapeutic Intervention With Metastasis of Non-small Cell Lung Cancer.Cancer genomics & proteomicsReview
- Pathophysiological functions of Rnd proteins.Small GTPasesReview
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The two p190RhoGAP proteins, p190RhoGAP-A and -B, are key regulators of Rho GTPase signaling and are essential for actin cytoskeletal structure and contractility. Here we report the discovery of two evolutionarily conserved GTPase-like domains located in the 'middle domain', previously thought to be unstructured. Deletion of these domains reduces RhoGAP activity. Crystal structures, MANT-GTPγS binding, thermal denaturation, biochemical assays and sequence homology analysis all strongly support defects in nucleotide-binding activity. Analysis of p190RhoGAP proteins therefore indicates the presence of two previously unidentified domains which represent an emerging group of pseudoenzymes, the pseudoGTPases.A growing number of 'pseudoenzymes' with a regulatory role in signal transduction processes but without catalytic activity are being identified. Here, the authors identify two pseudoGTPase domains in p190RhoGAP, characterize them biochemically and structurally and show that they influence RhoGAP activity.
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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.