ArticlePloS one2012
The N-terminal DH-PH domain of Trio induces cell spreading and migration by regulating lamellipodia dynamics in a Rac1-dependent fashion.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 45 citations in OpenAlex.
- Endothelial RhoGEF Trio is involved in angiogenesis.Vascular biology (Bristol, England) · 2026Article
- De NovoHuman mutation · 2026Article
- Monoclonal antibody for phosphorylated TRIO Y2681 that helps predict prognosis of post-operative colorectal cancer patients.BJC reports · 2025Article
- Serine phosphorylation of the RhoGEF Trio stabilizes endothelial cell-cell junctions.Small GTPases · 2023Article
- Role of RhoG as a regulator of cellular functions: integrating insights on immune cell activation, migration, and functions.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2023Review
- Autoinhibition of the GEF activity of cytoskeletal regulatory protein Trio is disrupted in neurodevelopmental disorder-related genetic variants.The Journal of biological chemistry · 2022Article
- RhoGEF Trio Regulates Radial Migration of Projection Neurons via Its Distinct Domains.Neuroscience bulletin · 2022Article
- The RhoGEF Trio: A Protein with a Wide Range of Functions in the Vascular Endothelium.International journal of molecular sciences · 2021Review
- Trio family proteins as regulators of cell migration and morphogenesis in development and disease - mechanisms and cellular contexts.Journal of cell science · 2021Review
- Targeting Rac and Cdc42 GEFs in Metastatic Cancer.Frontiers in cell and developmental biology · 2020Review
- Rab6 regulates cell migration and invasion by recruiting Cdc42 and modulating its activity.Cellular and molecular life sciences : CMLS · 2019Article
- Centrosome guides spatial activation of Rac to control cell polarization and directed cell migration.Life science alliance · 2019Article
- Direct multiplex imaging and optogenetics of Rho GTPases enabled by near-infrared FRET.Nature chemical biology · 2018Article
- The Role of Trio, a Rho Guanine Nucleotide Exchange Factor, in Glomerular Podocytes.International journal of molecular sciences · 2018Article
- Intercellular adhesion molecule-1 augments myoblast adhesion and fusion through homophilic trans-interactions.Scientific reports · 2017Article
- Flow-induced endothelial cell alignment requires the RhoGEF Trio as a scaffold protein to polarize active Rac1 distribution.Molecular biology of the cell · 2017Article
- Regulation of circular dorsal ruffles, macropinocytosis, and cell migration by RhoG and its exchange factor, Trio.Molecular biology of the cell · 2017Article
- RhoB loss induces Rac1-dependent mesenchymal cell invasion in lung cells through PP2A inhibition.Oncogene · 2016Article
- Recent insights into endothelial control of leukocyte extravasation.Cellular and molecular life sciences : CMLS · 2016Review
- Rab23 promotes squamous cell carcinoma cell migration and invasion via integrin β1/Rac1 pathway.Oncotarget · 2016Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The guanine-nucleotide exchange factor Trio encodes two DH-PH domains that catalyze nucleotide exchange on Rac1, RhoG and RhoA. The N-terminal DH-PH domain is known to activate Rac1 and RhoG, whereas the C-terminal DH-PH domain can activate RhoA. The current study shows that the N-terminal DH-PH domain, upon expression in HeLa cells, activates Rac1 and RhoG independently from each other. In addition, we show that the flanking SH3 domain binds to the proline-rich region of the C-terminus of Rac1, but not of RhoG. However, this SH3 domain is not required for Rac1 or RhoG GDP-GTP exchange. Rescue experiments in Trio-shRNA-expressing cells showed that the N-terminal DH-PH domain of Trio, but not the C-terminal DH-PH domain, restored fibronectin-mediated cell spreading and migration defects that are observed in Trio-silenced cells. Kymograph analysis revealed that the N-terminal DH-PH domain, independent of its SH3 domain, controls the dynamics of lamellipodia. Using siRNA against Rac1 or RhoG, we found that Trio-D1-induced lamellipodia formation required Rac1 but not RhoG expression. Together, we conclude that the GEF Trio is responsible for lamellipodia formation through its N-terminal DH-PH domain in a Rac1-dependent manner during fibronectin-mediated spreading and migration.
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