ArticleProtein science : a publication of the Protein Society2011
Modulation of a GEF switch: autoinhibition of the intrinsic guanine nucleotide exchange activity of p115-RhoGEF.
Article in Protein science : a publication of the Protein Society, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 37 citations in OpenAlex.
- Guanine Nucleotide Exchange Factors and Small GTPases: Their Regulation and Functions, Diseases, and Therapeutic Targets.MedComm · 2025Review
- The RhoGEF protein Plekhg5 self-associates via its PH domain to regulate apical cell constriction.Molecular biology of the cell · 2024Article
- Integration of Chemoinformatics and Multi-Omics Analysis Defines ECT2 as a Potential Target for Cancer Drug Therapy.Biology · 2023Article
- Characterization and computational simulation of human Syx, a RhoGEF implicated in glioblastoma.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Integrative multiomics and in silico analysis revealed the role of ARHGEF1 and its screened antagonist in mild and severe COVID-19 patients.Journal of cellular biochemistry · 2022Article
- GPCRs thatSmall GTPases · 2022Review
- Structural Design and Analysis of the RHOA-ARHGEF1 Binding Mode: Challenges and Applications for Protein-Protein Interface Prediction.Frontiers in molecular biosciences · 2021Article
- Multiplexed GTPase and GEF biosensor imaging enables network connectivity analysis.Nature chemical biology · 2020Article
- Optogenetic Control of RhoA to Probe Subcellular Mechanochemical Circuitry.Current protocols in cell biology · 2020Article
- Crystal structures of the PH domains from Lbc family of RhoGEFs bound to activated RhoA GTPase.Data in brief · 2018Article
- Secondary PDZ domain-binding site on class B plexins enhances the affinity for PDZ-RhoGEF.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Understanding the roles of FAK in cancer: inhibitors, genetic models, and new insights.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2015Review
- Intramolecular interactions between the Dbl homology (DH) domain and the carboxyl-terminal region of myosin II-interacting guanine nucleotide exchange factor (MyoGEF) act as an autoinhibitory mechanism for the regulation of MyoGEF functions.The Journal of biological chemistry · 2014Article
- The crystal structure of the RhoA-AKAP-Lbc DH-PH domain complex.The Biochemical journal · 2014Article
- Tyrosine phosphorylation of Dbl regulates GTPase signaling.The Journal of biological chemistry · 2014Article
- Modification of p115RhoGEF Ser(330) regulates its RhoGEF activity.Cellular signalling · 2013Article
- Activated RhoA is a positive feedback regulator of the Lbc family of Rho guanine nucleotide exchange factor proteins.The Journal of biological chemistry · 2013Article
- Structural basis for autoinhibition of the guanine nucleotide exchange factor FARP2.Structure (London, England : 1993) · 2013Article
- Structural determinants of RGS-RhoGEF signaling critical to Entamoeba histolytica pathogenesis.Structure (London, England : 1993) · 2013Article
- Structure of the Rho-specific guanine nucleotide-exchange factor Xpln.Acta crystallographica. Section F, Structural biology and crystallization communications · 2012Article
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Authors and funding
4 authors at 4 institutions in 1 country.
Funding
Abstract
p115-RhoGEF (p115) belongs to the family of RGS-containing guanine nucleotide exchange factors for Rho GTPases (RGS-RhoGEFs) that are activated by G12 class heterotrimeric G protein α subunits. All RGS-RhoGEFs possess tandemly linked Dbl-homology (DH) and plekstrin-homology (PH) domains, which bind and catalyze the exchange of GDP for GTP on RhoA. We have identified that the linker region connecting the N-terminal RGS-homology (RH) domain and the DH domain inhibits the intrinsic guanine nucleotide exchange (GEF) activity of p115, and determined the crystal structures of the DH/PH domains in the presence or absence of the inhibitory linker region. An N-terminal extension of the canonical DH domain (the GEF switch), which is critical to GEF activity, is well folded in the crystal structure of DH/PH alone, but becomes disordered in the presence of the linker region. The linker region is completely disordered in the crystal structure and partially disordered in the molecular envelope calculated from measurements of small angle x-ray scattering (SAXS). It is possible that Gα subunits activate p115 in part by relieving autoinhibition imposed by the linker region.
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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.