ArticleThe Journal of biological chemistry2010
Transforming growth factor beta-activated kinase 1 (TAK1) kinase adaptor, TAK1-binding protein 2, plays dual roles in TAK1 signaling by recruiting both an activator and an inhibitor of TAK1 kinase in tumor necrosis factor signaling pathway.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 72 citations in OpenAlex.
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- Regulation of RIPK1 Phosphorylation: Implications for Inflammation, Cell Death, and Therapeutic Interventions.Biomedicines · 2024Review
- Protein phosphatase 6 activates NF-κB to confer sensitivity to MAPK pathway inhibitors inScience signaling · 2024Article
- Cellular Dynamics of Fas-Associated Death Domain in the Regulation of Cancer and Inflammation.International journal of molecular sciences · 2024Review
- The Mechanism of Leptin Resistance in Obesity and Therapeutic Perspective.Advances in experimental medicine and biology · 2024Review
- Effects of TmTak1 silencing on AMP production as an Imd pathway component in Tenebrio molitor.Scientific reports · 2023Article
- The influence of selected microRNAs on the expression profile of genes and proteins related to the tumor necrosis factor-alpha signaling pathways in endometrioid endometrial cancer.Journal of cancer research and clinical oncology · 2023Article
- Inducible protein degradation as a strategy to identify Phosphoprotein Phosphatase 6 substrates in RAS-mutant colorectal cancer cells.bioRxiv : the preprint server for biology · 2023Article
- Aberrantly activated TAK1 links neuroinflammation and neuronal loss in Alzheimer's disease mouse models.Journal of cell science · 2023Article
- Mechanisms of TNF-independent RIPK3-mediated cell death.The Biochemical journal · 2022Review
- Deficiency of PPP6C protects TNF-induced necroptosis through activation of TAK1.Cell death & disease · 2022Article
- TAB2 deficiency induces dilated cardiomyopathy by promoting RIPK1-dependent apoptosis and necroptosis.The Journal of clinical investigation · 2022Article
- Circular RNA WHSC1 exerts oncogenic properties by regulating miR-7/TAB2 in lung cancer.Journal of cellular and molecular medicine · 2021Article
- The microRNA miR-133b functions to slow Duchenne muscular dystrophy pathogenesis.The Journal of physiology · 2021Article
- Toll-like receptor-mediated innate immunity against herpesviridae infection: a current perspective on viral infection signaling pathways.Virology journal · 2020Review
- Current translational potential and underlying molecular mechanisms of necroptosis.Cell death & disease · 2019Review
- TAK1 mediates convergence of cellular signals for death and survival.Apoptosis : an international journal on programmed cell death · 2019Review
- Gal-3BP Negatively Regulates NF-κB Signaling by Inhibiting the Activation of TAK1.Frontiers in immunology · 2019Article
- EnterohemorrhagicEmerging microbes & infections · 2019Article
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
Abstract
Transforming growth factor beta-activated kinase 1 (TAK1) kinase is an indispensable signaling intermediate in tumor necrosis factor (TNF), interleukin 1, and Toll-like receptor signaling pathways. TAK1-binding protein 2 (TAB2) and its closely related protein, TAB3, are binding partners of TAK1 and have previously been identified as adaptors of TAK1 that recruit TAK1 to a TNF receptor signaling complex. TAB2 and TAB3 redundantly mediate activation of TAK1. In this study, we investigated the role of TAB2 by analyzing fibroblasts having targeted deletion of the tab2 gene. In TAB2-deficient fibroblasts, TAK1 was associated with TAB3 and was activated following TNF stimulation. However, TAB2-deficient fibroblasts displayed a significantly prolonged activation of TAK1 compared with wild type control cells. This suggests that TAB2 mediates deactivation of TAK1. We found that a TAK1-negative regulator, protein phosphatase 6 (PP6), was recruited to the TAK1 complex in wild type but not in TAB2-deficient fibroblasts. Furthermore, we demonstrated that both PP6 and TAB2 interacted with the polyubiquitin chains and this interaction mediated the assembly with TAK1. Our results indicate that TAB2 not only activates TAK1 but also plays an essential role in the deactivation of TAK1 by recruiting PP6 through a polyubiquitin chain-dependent mechanism.
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