ArticleJournal of cell science2021
TRIP6 is required for tension at adherens junctions.
Article in Journal of cell science, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Mechanobiology of the Hippo-YAP Signaling Network.Cold Spring Harbor perspectives in biology · 2026Article
- Regulation of tension-dependent localization of LATS1 and LATS2 to adherens junctions.PloS one · 2026Article
- The ability of the LIMD1 and TRIP6 LIM domains to bind strained f-actin is critical for their tension dependent localization to adherens junctions and association with the Hippo pathway kinase LATS1.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Characterization of NOD-like receptor-based molecular heterogeneity in glioma and its association with immune micro-environment and metabolism reprogramming.Frontiers in immunology · 2024Article
- Article
- Mechanical regulation of cell-cycle progression and division.Trends in cell biology · 2022Review
- Förster resonance energy transfer efficiency of the vinculin tension sensor in cultured primary cortical neuronal growth cones.Neurophotonics · 2022Article
- Analysis of the Drosophila Ajuba LIM protein defines functions for distinct LIM domains.PloS one · 2022Article
- AJUBA and WTIP can compete with LIMD1 for junctional localization and LATS regulation.microPublication biology · 2022Article
- Endothelial YAP/TAZ Signaling in Angiogenesis and Tumor Vasculature.Frontiers in oncology · 2020Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Hippo signaling mediates influences of cytoskeletal tension on organ growth. TRIP6 and LIMD1 have each been identified as being required for tension-dependent inhibition of the Hippo pathway LATS kinases and their recruitment to adherens junctions, but the relationship between TRIP6 and LIMD1 was unknown. Using siRNA-mediated gene knockdown, we show that TRIP6 is required for LIMD1 localization to adherens junctions, whereas LIMD1 is not required for TRIP6 localization. TRIP6, but not LIMD1, is also required for the recruitment of vinculin and VASP to adherens junctions. Knockdown of TRIP6 or vinculin, but not of LIMD1, also influences the localization of myosin and F-actin. In TRIP6 knockdown cells, actin stress fibers are lost apically but increased basally, and there is a corresponding increase in the recruitment of vinculin and VASP to basal focal adhesions. Our observations identify a role for TRIP6 in organizing F-actin and maintaining tension at adherens junctions that could account for its influence on LIMD1 and LATS. They also suggest that focal adhesions and adherens junctions compete for key proteins needed to maintain attachments to contractile F-actin.
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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.