ArticleThe Journal of cell biology2015
TAGLN2 regulates T cell activation by stabilizing the actin cytoskeleton at the immunological synapse.
Article in The Journal of cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed, 93 citations in OpenAlex.
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- TAGLN2-mediated Actin Cytoskeleton Stabilization Promotes Proliferation and Metastasis of Ovarian Carcinoma.Applied immunohistochemistry & molecular morphology : AIMM · 2025Article
- Surface CD69-Negative CD4 and CD8 Bone Marrow-Resident Human Memory T Cells.European journal of immunology · 2025Article
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- Gastrodin reduces myocardial ischemia/reperfusion injury via transgelin2/CNPase-mediated apoptosis regulation.Frontiers in pharmacology · 2025Article
- Exploring novel drug targets for erectile dysfunction through plasma proteome with genome.Sexual medicine · 2024Article
- Development of BCMA-Targeted Bispecific Natural Killer Cell Engagers for Multiple Myeloma Treatment.Antibodies (Basel, Switzerland) · 2024Article
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- Mechanoregulation and function of calponin and transgelin.Biophysics reviews · 2024Review
- Glucose-mediated mitochondrial reprogramming by cholesterol export at TM4SF5-enriched mitochondria-lysosome contact sites.Cancer communications (London, England) · 2024Article
- Exploring the mechanism of tetramethylpyrazine in the treatment of osteoarthritis based on network pharmacology.Frontiers in chemistry · 2024Article
4 more citing papers are in PubMed but not listed here.
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Authors and funding
15 authors at 6 institutions in 2 countries.
Funding
Abstract
The formation of an immunological synapse (IS) requires tight regulation of actin dynamics by many actin polymerizing/depolymerizing proteins. However, the significance of actin stabilization at the IS remains largely unknown. In this paper, we identify a novel function of TAGLN2--an actin-binding protein predominantly expressed in T cells--in stabilizing cortical F-actin, thereby maintaining F-actin contents at the IS and acquiring LFA-1 (leukocyte function-associated antigen-1) activation after T cell receptor stimulation. TAGLN2 blocks actin depolymerization and competes with cofilin both in vitro and in vivo. Knockout of TAGLN2 (TAGLN2(-/-)) reduced F-actin content and destabilized F-actin ring formation, resulting in decreased cell adhesion and spreading. TAGLN2(-/-) T cells displayed weakened cytokine production and cytotoxic effector function. These findings reveal a novel function of TAGLN2 in enhancing T cell responses by controlling actin stability at the IS.
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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.