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TGF-beta activated kinase 1/MAP3K7 binding protein 1

TAB1, TAK1-binding protein 1
The protein encoded by this gene was identified as a regulator of the MAP kinase kinase kinase MAP3K7/TAK1, which is known to mediate various intracellular signaling pathways, such as those induced by TGF beta, interleukin 1, and WNT-1. This protein interacts and thus activates TAK1 kinase. It has been shown that the C-terminal portion of this protein is sufficient for binding and activation of TAK1, while a portion of the N-terminus acts as a dominant-negative inhibitor of TGF beta, suggesting that this protein may function as a mediator between TGF beta receptors and TAK1. This protein can also interact with and activate the mitogen-activated protein kinase 14 (MAPK14/p38alpha), and thus represents an alternative activation pathway, in addition to the MAPKK pathways, which contributes to the biological responses of MAPK14 to various stimuli. Alternatively spliced transcript variants encoding distinct isoforms have been reported. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: TAK1, p38, MAPK, NF-kappaB, V1a
Papers using TAB1 antibodies
c-Jun N-terminal kinase phosphorylates DCP1a to control formation of P bodies.
Debinski Waldemar, In PLoS ONE, 2010
... 13.1) all from Roche, FLAG M2 (F1804, Sigma), P(T180/Y182)-p38 MAPK (36–850, Invitrogen), P(T180)-p38 MAPK (02504), P(S438)-TAB1 (09519) both from Acris, TAK1 (4505), P(T187)-TAK1 (4536), ...
TAK1, but not TAB1 or TAB2, plays an essential role in multiple signaling pathways in vivo
Borthwick Lee A. et al., In The American Journal of Pathology, 2004
... Cell Signaling), Iκ-Bα (sc-1643; Santa Cruz Biotechnology), phospho-c-Jun (2361; Cell Signaling), c-Jun (9165; Cell Signaling), TAB1 (3226; Cell Signaling), TAB2 (3745; Cell Signaling), ...
Papers on TAB1
PGC-1β suppresses saturated fatty acid-induced macrophage inflammation by inhibiting TAK1 activation.
Xia et al., Guangzhou, China. In Iubmb Life, Feb 2016
Mechanistically, we revealed that TGF-β-activated kinase 1 (TAK1) and its adaptor protein TAK1 binding protein 1 (TAB1) played a dominant role in the regulatory effects of PGC-1β.
Identification and characterization of a TAB1 gene involved in innate immunity of amphioxus (Branchiostoma belcheri).
Jin et al., Nanjing, China. In Gene, Feb 2016
TAK1-binding protein, TAB1, can specifically regulate the activation of TAK1.
TRAF2-mediated Lys63-linked ubiquitination of DUSP14/MKP6 is essential for its phosphatase activity.
Tan et al., Taiwan. In Cell Signal, Jan 2016
We recently reported that DUSP14 negatively regulates T-cell activation and immune responses by interfering activation of TAB1-TAK1 complex.
Docosahexaenoic acid inhibits inflammation via Free Fatty Acid Receptor FFA4, disruption of TAB2 interaction with TAK1/TAB1, and down-regulation of ERK-dependent Egr-1 expression in EA.hy926 cells.
Chen et al., T'ai-chung-shih, Taiwan. In Mol Nutr Food Res, Dec 2015
METHODS AND RESULTS: TNFα markedly induced the interaction between TAK1 binding protein (TAB) 2 and TAK1/TAB1, the phosphorylation of ERK, p38 MAPK, and Akt, the expression of Egr-1 and ICAM-1, and HL-60 (monocyte-like) cell adhesion.
Ubiquitin plays an atypical role in GPCR-induced p38 MAP kinase activation on endosomes.
Trejo et al., San Diego, United States. In J Cell Biol, Oct 2015
TAB2 associated with TAB1, which induced p38 activation independent of MKK3 and MKK6.
The kinase p38 activated by the metabolic regulator AMPK and scaffold TAB1 drives the senescence of human T cells.
Akbar et al., London, United Kingdom. In Nat Immunol, 2014
Here we found that senescent human T cells lacked the canonical and alternative pathways for the activation of p38 but spontaneously engaged the metabolic master regulator AMPK to trigger recruitment of p38 to the scaffold protein TAB1, which caused autophosphorylation of p38.
TAK1 regulates hepatic cell survival and carcinogenesis.
Seki et al., San Diego, United States. In J Gastroenterol, 2014
TAK1 activity is tightly regulated by its binding proteins, TAB1 and TAB2/TAB3, as well as by post-translational modification including ubiquitination and phosphorylation.
Omega-3 Fatty Acids and FFAR4.
Walenta et al., San Diego, United States. In Front Endocrinol (lausanne), 2013
This makes FFAR4 to be capable of interacting with β-arrestin-2, which in turn, results in association of β-arrestin-2 with TAB1.
c-Abl promotes osteoblast expansion by differentially regulating canonical and non-canonical BMP pathways and p16INK4a expression.
Li et al., Shanghai, China. In Nat Cell Biol, 2012
c-Abl interacts with and phosphorylates BMPRIA and the phosphorylation differentially influences the interaction of BMPRIA with BMPRII and the Tab1-Tak1 complex, leading to uneven activation of Smad1/5/8 and Erk1/2, the canonical and non-canonical BMP pathways that direct the expression of p16(INK4a).
The critical role of TAK1 in accentuated epithelial to mesenchymal transition in obliterative bronchiolitis after lung transplantation.
Borthwick et al., Newcastle upon Tyne, United Kingdom. In Am J Pathol, 2012
TAK1 plays a critical role in accentuated epithelial to mesenchymal transition in obliterative bronchiolitis after lung transplantation.
O-GlcNAcylation of TAB1 modulates TAK1-mediated cytokine release.
van Aalten et al., Dundee, United Kingdom. In Embo J, 2012
O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress.
Epithelial transforming growth factor β-activated kinase 1 (TAK1) is activated through two independent mechanisms and regulates reactive oxygen species.
Ninomiya-Tsuji et al., Raleigh, United States. In Proc Natl Acad Sci U S A, 2012
Epithelial TAK1 activity is regulated through two unique, TAB1-dependent basal & TAB2-mediated stimuli-dependent mechanisms.
TLR-signaling networks: an integration of adaptor molecules, kinases, and cross-talk.
Martin et al., Louisville, United States. In J Dent Res, 2011
ABBREVIATIONS: TLR, Toll-like receptor; PRR, pattern recognition receptor; PAMP, pathogen-associated molecular pattern; LPS, lipopolysaccharide; APC, antigen-presenting cell; IL, interleukin; TIR, Toll/IL-1R homology; MyD88, myeloid differentiation factor 88; IFN, interferon; TRIF, TIR-domain-containing adapter-inducing interferon-β; IRAK, IL-1R-associated kinase; TAK1, TGF-β-activated kinase; TAB1, TAK1-binding protein; NF-κB, nuclear factor kappa-light-chain-enhancer of activated B-cells; MAPK, mitogen-activated protein kinase; NLR, NOD-like receptors; LRR, leucine-rich repeats; DC, dendritic cell; PI3K, phosphoinositide 3-kinases; GSK3, glycogen synthase kinase-3; mTOR, mammalian target of rapamycin; DAF, decay-accelerating factor; IKK, IκB kinase; IRF, interferon regulatory factors; TBK1, TANK-binding kinase 1; CARD, caspase activation and recruitment domain; PYD, pyrin N-terminal homology domain; ATF, activating transcription factor; and PTEN, phosphatase and tensin homolog.
A small peptide modeled after the NRAGE repeat domain inhibits XIAP-TAB1-TAK1 signaling for NF-κB activation and apoptosis in P19 cells.
Verdi et al., United States. In Plos One, 2010
XIAP-TAB1-TAK1 complex is dependent on NRAGE for IKK-alpha/beta phosphorylation and NF-kappaB activation.
Identification and functional characterization of novel phosphorylation sites in TAK1-binding protein (TAB) 1.
Kracht et al., Gießen, Germany. In Plos One, 2010
data suggest a complex role of aa 452-457 of TAB1 in controlling p38 MAPK activity and subcellular localization and implicate these residues in TAK1- or p38 MAPK-dependent post-transcriptional control of gene expression
Molecular switching of osteoblastogenesis versus adipogenesis: implications for targeted therapies.
Kato et al., Tokyo, Japan. In Expert Opin Ther Targets, 2009
In the first pathway, the TNF-alpha- or IL-1-induced TAK1/TAB1/NIK signaling cascade attenuates PPAR-gamma-mediated adipogenesis by inhibiting the binding of PPAR-gamma to the DNA response element.
Interaction between TAK1-TAB1-TAB2 and RCAN1-calcineurin defines a signalling nodal control point.
Molkentin et al., Cincinnati, United States. In Nat Cell Biol, 2009
Here we performed a yeast two-hybrid screen with RCAN1 as bait, identifying TAK1 binding protein 2 (TAB2) as an interacting partner.
Suppression of PPAR transactivation switches cell fate of bone marrow stem cells from adipocytes into osteoblasts.
Kato et al., Tokyo, Japan. In Ann N Y Acad Sci, 2007
One signaling is a TAK1/TAB1/NIK cascade activated by TNF-alpha and IL-1, and the activated NF-kappaB blocked the DNA binding of PPAR-gamma, attenuating the activated PPAR-mediated adipogenesis.
Cytokines suppress adipogenesis and PPAR-gamma function through the TAK1/TAB1/NIK cascade.
Kato et al., Tokyo, Japan. In Nat Cell Biol, 2003
Here we show that the ligand-induced transactivation function of PPAR-gamma is suppressed by IL-1 and TNF-alpha, and that this suppression is mediated through NF-kappaB activated by the TAK1/TAB1/NF-kappaB-inducing kinase (NIK) cascade, a downstream cascade associated with IL-1 and TNF-alpha signalling.
MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha.
Han et al., Los Angeles, United States. In Science, 2002
interaction with p38alpha leads to autophosphorylation and activation of p38alpha
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