Phosphorylation‐dependent activation of TAK1 mitogen‐activated protein kinase kinase kinase by TAB1

Sakurai, Hiroaki; Miyoshi, Hidetaka; Mizukami, Junko; Sugita, Takahisa

doi:10.1016/s0014-5793(00)01588-x

Cited by 161 publications

(139 citation statements)

References 19 publications

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“…However, some studies have shown that the phosphorylation of these sites is insufficient for TAK1 activation (14,15). Consistent with this notion, our recent investigation with PP1 implied that the phosphorylation of TAK1 Ser-412 is important for TAK1 activation and function (30).…”

Section: The Phosphorylation Of Tak1 Ser-412 Is Essential For Tlrsupporting

confidence: 77%

“…In particular, the phosphorylation of residues Thr-184 and Thr-187 located at the TAK1 kinase domain is required for TAK1 kinase activity (10,11). However, a few researchers have suggested that the phosphorylation of TAK1 Thr-187 is insufficient for its activation (12)(13)(14)(15). Thus, additional post-transla-tional modifications are needed.…”

Section: Tgf-␤-activated Kinase 1 (Tak1) Is a Key Kinase In Mediatingmentioning

confidence: 99%

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Transforming Growth Factor (TGF)-β-activated Kinase 1 (TAK1) Activation Requires Phosphorylation of Serine 412 by Protein Kinase A Catalytic Subunit α (PKACα) and X-linked Protein Kinase (PRKX)

Ouyang

Nie

et al. 2014

Journal of Biological Chemistry

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Background: Understanding of molecular mechanism of TAK1 activation is incomplete. Results: PKAC␣ and PRKX phosphorylate TAK1 at serine 412 to regulate TAK1 activation in the IL-1 receptor (IL-1R) and Toll-like receptor (TLR) signaling pathways. Conclusion: TAK1 activation requires phosphorylation by PKAC␣ and PRKX. Significance: This study advanced our understanding of the molecular mechanism of TAK1 activation.

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Section: The Phosphorylation Of Tak1 Ser-412 Is Essential For Tlrsupporting

confidence: 77%

Section: Tgf-␤-activated Kinase 1 (Tak1) Is a Key Kinase In Mediatingmentioning

confidence: 99%

Transforming Growth Factor (TGF)-β-activated Kinase 1 (TAK1) Activation Requires Phosphorylation of Serine 412 by Protein Kinase A Catalytic Subunit α (PKACα) and X-linked Protein Kinase (PRKX)

Ouyang

Nie

et al. 2014

Journal of Biological Chemistry

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“…5C). We also noted that total TAK1 expression was reduced by TAB1 siRNA, but not by control siRNA, perhaps because TAB1 exists in a 1:1 stoichiometric complex with TAK1 (68) and that activation has a correlation with its stability (29). TAB1 siRNA blocked TGF-␤1-induced TAK1 phosphorylation at Thr-187 but did not alter TGF-␤1-induced Smad2/3 phosphorylation.…”

Section: Tab1 Mediates Tgf-␤1-induced Tak1mentioning

confidence: 67%

Transforming Growth Factor-β (TGF-β1) Activates TAK1 via TAB1-mediated Autophosphorylation, Independent of TGF-β Receptor Kinase Activity in Mesangial Cells

Kim

Kwak

et al. 2009

Journal of Biological Chemistry

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Transforming growth factor-␤1 (TGF-␤1) is a multifunctional cytokine that signals through the interaction of type I (T␤RI) and type II (T␤RII) receptors to activate distinct intracellular pathways. TAK1 is a serine/threonine kinase that is rapidly activated by TGF-␤1. However, the molecular mechanism of TAK1 activation is incompletely understood. Here, we propose a mechanism whereby TAK1 is activated by TGF-␤1 in primary mouse mesangial cells. Under unstimulated conditions, endogenous TAK1 is stably associated with T␤RI. TGF-␤1 stimulation causes rapid dissociation from the receptor and induces TAK1 phosphorylation. Deletion mutant analysis indicates that the juxtamembrane region including the GS domain of T␤RI is crucial for its interaction with TAK1. Both T␤RI-mediated TAK1 phosphorylation and TGF-␤1-induced TAK1 phosphorylation do not require kinase activity of T␤RI. Moreover, T␤RI-mediated TAK1 phosphorylation correlates with the degree of its association with T␤RI and requires kinase activity of TAK1. TAB1 does not interact with TGF-␤ receptors, but TAB1 is indispensable for TGF-␤1-induced TAK1 activation. We also show that TRAF6 and TAB2 are required for the interaction of TAK1 with T␤RI and TGF-␤1-induced TAK1 activation in mouse mesangial cells. Taken together, our data indicate that TGF-␤1-induced interaction of T␤RI and T␤RII triggers dissociation of TAK1 from T␤RI, and subsequently TAK1 is phosphorylated through TAB1-mediated autophosphorylation and not by the receptor kinase activity of T␤RI.

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“…Proinflammatory cytokines, such as TNF-α and interleukin 1 (IL-1), activate downstream signals in a manner mediated by TGF-β-activated kinase I (TAK1), also known as mitogen-activated protein kinase kinase kinase 7 (Sakurai et al 2000;Wang et al 2001). A recent study showed that O-GlcNAcylation of TAK1-binding protein (TAB1) modulates TAK1-mediated cytokine release when induced by IL-1 and osmotic stress (Pathak et al 2012).…”

Section: Inflammationmentioning

confidence: 99%

Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis

Groves

Lee

Yildirir

et al. 2013

Cell Stress and Chaperones

120

112

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O-linked N-acetyl-β-D-glucosamine (O-GlcNAc) is a ubiquitous and dynamic post-translational modification known to modify over 3,000 nuclear, cytoplasmic, and mitochondrial eukaryotic proteins. Addition of O-GlcNAc to proteins is catalyzed by the O-GlcNAc transferase and is removed by a neutral-N-acetyl-β-glucosaminidase (OGlcNAcase). O-GlcNAc is thought to regulate proteins in a manner analogous to protein phosphorylation, and the cycling of this carbohydrate modification regulates many cellular functions such as the cellular stress response. Diverse forms of cellular stress and tissue injury result in enhanced O-GlcNAc modification, or O-GlcNAcylation, of numerous intracellular proteins. Stress-induced OGlcNAcylation appears to promote cell/tissue survival by regulating a multitude of biological processes including: the phosphoinositide 3-kinase/Akt pathway, heat shock protein expression, calcium homeostasis, levels of reactive oxygen species, ER stress, protein stability, mitochondrial dynamics, and inflammation. Here, we will discuss the regulation of these processes by O-GlcNAc and the impact of such regulation on survival in models of ischemia reperfusion injury and trauma hemorrhage. We will also discuss the misregulation of O-GlcNAc in diseases commonly associated with the stress response, namely Alzheimer's and Parkinson's diseases. Finally, we will highlight recent advancements in the tools and technologies used to study the O-GlcNAc modification.

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Phosphorylation‐dependent activation of TAK1 mitogen‐activated protein kinase kinase kinase by TAB1

Cited by 161 publications

References 19 publications

Transforming Growth Factor (TGF)-β-activated Kinase 1 (TAK1) Activation Requires Phosphorylation of Serine 412 by Protein Kinase A Catalytic Subunit α (PKACα) and X-linked Protein Kinase (PRKX)

Transforming Growth Factor (TGF)-β-activated Kinase 1 (TAK1) Activation Requires Phosphorylation of Serine 412 by Protein Kinase A Catalytic Subunit α (PKACα) and X-linked Protein Kinase (PRKX)

Transforming Growth Factor-β (TGF-β1) Activates TAK1 via TAB1-mediated Autophosphorylation, Independent of TGF-β Receptor Kinase Activity in Mesangial Cells

Dynamic O-GlcNAcylation and its roles in the cellular stress response and homeostasis

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