ArticleThe Journal of biological chemistry2016
Deciphering the Molecular and Functional Basis of RHOGAP Family Proteins: A SYSTEMATIC APPROACH TOWARD SELECTIVE INACTIVATION OF RHO FAMILY PROTEINS.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers, 1 of them a synthesis that pooled it.
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Who cites it
70 citing papers in PubMed, 1 synthesis or guideline pooled it, 111 citations in OpenAlex.
- The Significance of theFrontiers in oncology · 2020Pooled it
- Daam-, FMNL-, and mDia-family formins jointly regulate cortical actin dynamics in melanoma cells.Cell communication and signaling : CCS · 2026Article
- Identification ofInternational journal of molecular sciences · 2026Article
- Non-canonical and constitutive activation of small GTPases: more than an exception to the rule?The Biochemical journal · 2026Review
- The WNK-OXSR1 osmosensing pathway mediates intestinal regeneration via Hippo-YAP signaling.The EMBO journal · 2026Article
- The cytokinesis regulator RacGAP1 is a Rac1-specific GAP on membranes.Protein science : a publication of the Protein Society · 2026Article
- Mechanistic study of ARHGAP27 promoting the progression of aortic dissection by regulating the RhoA/ROCK/YAP pathway.Frontiers in cardiovascular medicine · 2026Article
- New insights into the classification of the RAC1 P29S hotspot mutation in melanoma as an oncogene.Cancer gene therapy · 2025Article
- Rho Small GTPase Family in Androgen-Regulated Prostate Cancer Progression and Metastasis.Cancers · 2025Review
- Molecular and genetic characterization of sex-linked orange coat color in the domestic cat.Current biology : CB · 2025Article
- Understanding the Role of Rho GTPase Activating Protein and Bone Marrow Kinase X: A Novel Target in Gastric Cancer Treatment.Asian Pacific journal of cancer prevention : APJCP · 2025Review
- Proximity-based proteomics (BioID) uncovers the Rho GTPase interactome in kidney podocytes.Frontiers in cell and developmental biology · 2025Article
- Loss of Arhgap39 facilitates cell migration and invasion in murine hepatocellular cancer cells.Oncology research · 2025Article
- C1-linker region of PARG1 RhoGAP promotes the catalytic recognition fold of RhoA substrate.PloS one · 2025Article
- Oscillatory dynamics of Rac1 activity in Dictyostelium discoideum amoebae.PLoS computational biology · 2024Article
- Early gastric cancer with RhoGAP fusion is linked to frequent nodal metastasis and a part of microtubular-mucocellular histology.Gastric cancer : official journal of the International Gastric Cancer Association and the Japanese Gastric Cancer Association · 2024Article
- DLC1 promotes mechanotransductive feedback for YAP via RhoGAP-mediated focal adhesion turnover.Journal of cell science · 2024Article
- Spatiotemporal regulation of Rho GTPase signaling during endothelial barrier remodeling.Current opinion in physiology · 2023Review
- A Structural Network Analysis of Neuronal ArhGAP21/23 Interactors by Computational Modeling.ACS omega · 2023Article
- Impact of alcohol exposure on neural development and network formation in human cortical organoids.Molecular psychiatry · 2023Article
10 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
RHO GTPase-activating proteins (RHOGAPs) are one of the major classes of regulators of the RHO-related protein family that are crucial in many cellular processes, motility, contractility, growth, differentiation, and development. Using database searches, we extracted 66 distinct human RHOGAPs, from which 57 have a common catalytic domain capable of terminating RHO protein signaling by stimulating the slow intrinsic GTP hydrolysis (GTPase) reaction. The specificity of the majority of the members of RHOGAP family is largely uncharacterized. Here, we comprehensively investigated the sequence-structure-function relationship between RHOGAPs and RHO proteins by combining our in vitro data with in silico data. The activity of 14 representatives of the RHOGAP family toward 12 RHO family proteins was determined in real time. We identified and structurally verified hot spots in the interface between RHOGAPs and RHO proteins as critical determinants for binding and catalysis. We have found that the RHOGAP domain itself is nonselective and in some cases rather inefficient under cell-free conditions. Thus, we propose that other domains of RHOGAPs confer substrate specificity and fine-tune their catalytic efficiency in cells.
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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.