Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling

Ishitani, Tohru

doi:10.1093/emboj/cdg605

Cited by 256 publications

(259 citation statements)

References 83 publications

(68 reference statements)

Supporting

Mentioning

247

Contrasting

Unclassified

Order By: Relevance

“…[30][31][32] TAB2 and TAB3 are close homologs, whereas TAB1 is structurally unrelated to TAB2 or TAB3. TAB1 and TAB2/TAB3 bind to the N-terminal kinase domain and the C-terminal region of TAK1, respectively.…”

Section: The Roles Of Tak1-binding Proteins In Tak1 Activationmentioning

confidence: 99%

“…18,24 Consistently, inhibition of TAB2 reduces TAK1 activity in several tissues and cell types. 32,36,37 However, Broglie et al 38 described that loss of Tab2 in dermal fibroblasts rather prolonged and increased the activation of TAK1 following TNFa stimulation. TAK1 is normally transiently activated by TNFa and deactivated by protein phosphatase 6 (PP6) 39 and protein phosphatase 2A.…”

Section: The Roles Of Tak1-binding Proteins In Tak1 Activationmentioning

confidence: 99%

See 1 more Smart Citation

TAK1 control of cell death

2014

View full text Add to dashboard Cite

Programmed cell death, a physiologic process for removing cells, is critically important in normal development and for elimination of damaged cells. Conversely, unattended cell death contributes to a variety of human disease pathogenesis. Thus, precise understanding of molecular mechanisms underlying control of cell death is important and relevant to public health. Recent studies emphasize that transforming growth factor-b-activated kinase 1 (TAK1) is a central regulator of cell death and is activated through a diverse set of intra-and extracellular stimuli. The physiologic importance of TAK1 and TAK1-binding proteins in cell survival and death has been demonstrated using a number of genetically engineered mice. These studies uncover an indispensable role of TAK1 and its binding proteins for maintenance of cell viability and tissue homeostasis in a variety of organs. TAK1 is known to control cell viability and inflammation through activating downstream effectors such as NF-jB and mitogen-activated protein kinases (MAPKs). It is also emerging that TAK1 regulates cell survival not solely through NF-jB but also through NF-jB-independent pathways such as oxidative stress and receptor-interacting protein kinase 1 (RIPK1) kinase activity-dependent pathway. Moreover, recent studies have identified TAK1's seemingly paradoxical role to induce programmed necrosis, also referred to as necroptosis. This review summarizes the consequences of TAK1 deficiency in different cell and tissue types from the perspective of cell death and also focuses on the mechanism by which TAK1 complex inhibits or promotes programmed cell death. This review serves to synthesize our current understanding of TAK1 in cell survival and death to identify promising directions for future research and TAK1's potential relevance to human disease pathogenesis.

show abstract

Section: The Roles Of Tak1-binding Proteins In Tak1 Activationmentioning

confidence: 99%

Section: The Roles Of Tak1-binding Proteins In Tak1 Activationmentioning

confidence: 99%

TAK1 control of cell death

2014

View full text Add to dashboard Cite

show abstract

“…[21][22][23][24] TRAF2 25,26 and cIAPs [27][28][29][30] catalyse the polyubiquitination of RIP1. The ubiquitin-decorated RIP1 is recognized by ubiquitin-binding domain containing proteins in the IkB kinase (IKK) 31 and TAK1 kinase complexes [32][33][34] thus facilitating TAK-1-mediated phosphorylation and activation of IKKs. The latter subsequently phosphorylate the IkB proteins, which normally sequester NFkB in an inactive state in the cytoplasm, resulting in ubiquitination and proteasomal degradation of IkB and allowing for nuclear translocation of the liberated NFkB.…”

Section: Rip1 and Tnf Signalling: Inflammation Versus Apoptosismentioning

confidence: 99%

RIP kinases: key decision makers in cell death and innate immunity

et al. 2014

View full text Add to dashboard Cite

“…To conclude, oligomerization of TRAF6 might lead to auto-polyubiquitination of TRAF6, which is necessary for IL-1-and LPS-induced NF-kB activation, whereas TRAF6-induced poly-ubiquitination of NEMO might rather play a role in IL-1-induced JNK activation. TAB1, TAB2 and TAB3 have been described as adaptors for TAK1 [48,53]. However, the role of TAB1 in IL-1-induced NF-kB activation has been argued.…”

Section: Il-1r and Tlr-4 Signaling To Nf-kbmentioning

confidence: 99%

TLR-4, IL-1R and TNF-R signaling to NF-κB: variations on a common theme

Verstrepen

Bekaert

Chau

et al. 2008

Cell. Mol. Life Sci.

386

297

View full text Add to dashboard Cite

Abstract. Toll-like receptors (TLRs) as well as the receptors for tumor necrosis factor (TNF-R) and interleukin-1 (IL-1R) play an important role in innate immunity by regulating the activity of distinct transcription factors such as nuclear factor-kB (NF-kB). TLR, IL-1R and TNF-R signaling to NF-kB converge on a common IkB kinase complex that phosphorylates the NF-kB inhibitory protein IkBa. However, upstream signaling components are in large part receptor-specific. Nevertheless, the principles of signaling are similar, involving the recruitment of specific adaptor proteins and the activation of kinase cascades in which protein-protein interactions are controlled by poly-ubiquitination. In this review, we will discuss our current knowledge of NF-kB signaling in response to TLR-4, TNF-R and IL-1R stimulation, with a special focus on the similarities and dissimilarities among these pathways.Keywords. Toll-like receptor 4, interleukin-1, tumor necrosis factor, NF-kB, signal transduction. NF-kB, does it still need to be introduced?Nuclear factor kB (NF-kB) is the generic name of a family of transcription factors that regulate the expression of a large number of genes involved in immune and inflammatory responses, as well as in cell survival, cell proliferation and cell differentiation. NFkB transcription factors are activated in response to various stimuli, including cytokines, infectious agents, injury and other stressful conditions requiring rapid reprogramming of gene expression. Inappropriate activation of the NF-kB signaling pathway is implicated in the pathogenesis of chronic inflammation and autoimmunity, certain hereditary disorders and various cancers. In mammals, the NF-kB family consists of five proteins sharing a highly conserved Rel homology domain: c-Rel, RelB, p65 (= RelA), p105 (= NF-kB1) and p100 (=NF-kB2). The first three contain Cterminal transactivation domains, while the others share a long C-terminal domain with multiple copies of ankyrin repeats, which inhibit their activation.

show abstract

Role of the TAB2-related protein TAB3 in IL-1 and TNF signaling

Cited by 256 publications

References 83 publications

TAK1 control of cell death

TAK1 control of cell death

RIP kinases: key decision makers in cell death and innate immunity

TLR-4, IL-1R and TNF-R signaling to NF-κB: variations on a common theme

Contact Info

Product

Resources

About