ArticleThe Journal of biological chemistry2007
PTPL1/FAP-1 negatively regulates TRIP6 function in lysophosphatidic acid-induced cell migration.
Article in The Journal of biological chemistry, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 40 citations in OpenAlex.
- TRIP6 promotes inflammatory damage via the activation of TRAF6 signaling in a murine model of DSS-induced colitis.Journal of inflammation (London, England) · 2022Article
- Dual Role of the PTPN13 Tyrosine Phosphatase in Cancer.Biomolecules · 2020Review
- [Research progress on the biological regulatory function of lysophosphatidic acid in bone tissue cells].Hua xi kou qiang yi xue za zhi = Huaxi kouqiang yixue zazhi = West China journal of stomatology · 2020Review
- TRIP6 enhances stemness property of breast cancer cells through activation of Wnt/β-catenin.Cancer cell international · 2020Article
- PTPN13 induces cell junction stabilization and inhibits mammary tumor invasiveness.Theranostics · 2020Article
- LPADevelopmental dynamics : an official publication of the American Association of Anatomists · 2019Article
- Autotaxin-Lysophosphatidic Acid: From Inflammation to Cancer Development.Mediators of inflammation · 2017Review
- Novel Inhibitory Effect of a Lysophosphatidic Acid 2 Agonist on Allergen-Driven Airway Inflammation.American journal of respiratory cell and molecular biology · 2016Article
- The Cell Adhesion Molecule Necl-4/CADM4 Serves as a Novel Regulator for Contact Inhibition of Cell Movement and Proliferation.PloS one · 2015Article
- Lysophospholipid receptor nomenclature review: IUPHAR Review 8.British journal of pharmacology · 2014Review
- LPA receptor signaling: pharmacology, physiology, and pathophysiology.Journal of lipid research · 2014Review
- Characterization of TRIP6-dependent nasopharyngeal cancer cell migration.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2013Article
- Virtual screening for LPA2-specific agonists identifies a nonlipid compound with antiapoptotic actions.Molecular pharmacology · 2012Article
- Downregulation of protein tyrosine phosphatase PTPL1 alters cell cycle and upregulates invasion-related genes in prostate cancer cells.Clinical & experimental metastasis · 2012Article
- TRIP6: an adaptor protein that regulates cell motility, antiapoptotic signaling and transcriptional activity.Cellular signalling · 2011Review
- PTPN13/PTPL1: an important regulator of tumor aggressiveness.Anti-cancer agents in medicinal chemistry · 2011Review
- The adaptor protein TRIP6 antagonizes Fas-induced apoptosis but promotes its effect on cell migration.Molecular and cellular biology · 2010Article
- PTPL1/PTPN13 regulates breast cancer cell aggressiveness through direct inactivation of Src kinase.Cancer research · 2010Article
- Supervillin reorganizes the actin cytoskeleton and increases invadopodial efficiency.Molecular biology of the cell · 2009Article
- Regulation of the LPA2 receptor signaling through the carboxyl-terminal tail-mediated protein-protein interactions.Biochimica et biophysica acta · 2008Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The LIM domain-containing TRIP6 (Thyroid Hormone Receptor-interacting Protein 6) is a focal adhesion molecule known to regulate lysophosphatidic acid (LPA)-induced cell migration through interaction with the LPA2 receptor. LPA stimulation targets TRIP6 to the focal adhesion complexes and promotes c-Src-dependent phosphorylation of TRIP6 at Tyr-55, which creates a docking site for the Crk Src homology 2 domain, thereby promoting LPA-induced morphological changes and cell migration. Here we further demonstrate that a switch from c-Src-mediated phosphorylation to PTPL1/Fas-associated phosphatase-1-dependent dephosphorylation serves as an inhibitory feedback control mechanism of TRIP6 function in LPA-induced cell migration. PTPL1 dephosphorylates phosphotyrosine 55 of TRIP6 in vitro and inhibits LPA-induced tyrosine phosphorylation of TRIP6 in cells. This negative regulation requires a direct protein-protein interaction between these two molecules and the phosphatase activity of PTPL1. In contrast to c-Src, PTPL1 prevents TRIP6 turnover at the sites of adhesions. As a result, LPA-induced association of TRIP6 with Crk and the function of TRIP6 to promote LPA-induced morphological changes and cell migration are inhibited by PTPL1. Together, these results reveal a novel mechanism by which PTPL1 phosphatase plays a counteracting role in regulating TRIP6 function in LPA-induced cell migration.
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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.