ArticleProceedings of the National Academy of Sciences of the United States of America1996
The multidomain protein Trio binds the LAR transmembrane tyrosine phosphatase, contains a protein kinase domain, and has separate rac-specific and rho-specific guanine nucleotide exchange factor domains.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 181 papers.
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Who cites it
181 citing papers in PubMed, 464 citations in OpenAlex.
- Identification and growth features of developmental delay with macrocephaly caused by a novel TRIO variant affecting the second SH3 domain.BMC medical genomics · 2026Article
- Recent advances in the molecular genetic mechanisms and immune microenvironment of uveal melanoma.Melanoma research · 2026Review
- Endothelial RhoGEF Trio is involved in angiogenesis.Vascular biology (Bristol, England) · 2026Article
- Synaptic Cell Adhesion: A Structural Perspective.Advances in neurobiology · 2026Review
- Rho signaling promotes cell excitability and synaptic transmission.bioRxiv : the preprint server for biology · 2025Article
- MIG-21 interacts with Wnt and Netrin signaling in gonad migration in C. elegans.PLoS genetics · 2025Article
- Monoclonal antibody for phosphorylated TRIO Y2681 that helps predict prognosis of post-operative colorectal cancer patients.BJC reports · 2025Article
- Blocking YAP1-Liprin-β2 interaction impedes metastasis and promotes tumor suppression in head and neck squamous carcinoma.Scientific reports · 2025Article
- Article
- Rare missense variants of the leukocyte common antigen related receptor (LAR) display reduced activity in transcellular adhesion and synapse formation.Research square · 2025Article
- The Rho GEF Trio functions in contact inhibition of locomotion of neural crest cells by interacting with Ptk7.Development (Cambridge, England) · 2025Article
- Both GEF domains of the autism and developmental epileptic encephalopathy-associated Trio protein are required for proper tangential migration of GABAergic interneurons.Molecular psychiatry · 2025Article
- MIG-21 is a novel regulator of Wnt and Netrin signaling in gonad migration identified from published scRNA-seq data and functionally validated inbioRxiv : the preprint server for biology · 2025Article
- Rare missense variants of the leukocyte common antigen related receptor (LAR) display reduced activity in transcellular adhesion and synapse formation.bioRxiv : the preprint server for biology · 2025Article
- Common Genetic Variants inGenetics research · 2025Article
- Collaborative Roles for RAC1, ERM Proteins and PTEN During Adult Sensory Axon Regeneration.Molecular neurobiology · 2025Article
- New Mechanisms Underlying Oncogenesis in Dbl Family Rho Guanine Nucleotide Exchange Factors.Molecular pharmacology · 2024Review
- The RNA-binding protein Nab2 regulates levels of the RhoGEF Trio to govern axon and dendrite morphology.Molecular biology of the cell · 2024Article
- Serine phosphorylation of the RhoGEF Trio stabilizes endothelial cell-cell junctions.Small GTPases · 2023Article
- The organization and function of the Golgi apparatus in dendrite development and neurological disorders.Genes & diseases · 2023Review
121 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
rho-like GTP binding proteins play an essential role in regulating cell growth and actin polymerization. These molecular switches are positively regulated by guanine nucleotide exchange factors (GEFs) that promote the exchange of GDP for GTP. Using the interaction-trap assay to identify candidate proteins that bind the cytoplasmic region of the LAR transmembrane protein tyrosine phosphatase (PT-Pase), we isolated a cDNA encoding a 2861-amino acid protein termed Trio that contains three enzyme domains: two functional GEF domains and a protein serine/threonine kinase (PSK) domain. One of the Trio GEF domains (Trio GEF-D1) has rac-specific GEF activity, while the other Trio GEF domain (Trio GEF-D2) has rho-specific activity. The C-terminal PSK domain is adjacent to an Ig-like domain and is most similar to calcium/calmodulin-dependent kinases, such as smooth muscle myosin light chain kinase which similarly contains associated Ig-like domains. Near the N terminus, Trio has four spectrin-like repeats that may play a role in intracellular targeting. Northern blot analysis indicates that Trio has a broad tissue distribution. Trio appears to be phosphorylated only on serine residues, suggesting that Trio is not a LAR substrate, but rather that it forms a complex with LAR. As the LAR PTPase localizes to the ends of focal adhesions, we propose that LAR and the Trio GEF/PSK may orchestrate cell-matrix and cytoskeletal rearrangements necessary for cell migration.
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