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TAK1 (show MAP3K7 Proteins)/TAB1 expression in non-small cell lung carcinoma tissue is significantly increased and closely associated with patient clinical prognosis.
miR (show MLXIP Proteins)-29a repressed TAB1-mediated TIMP-1 (show TIMP1 Proteins) production in dermal fibroblasts, demonstrating that miR (show MLXIP Proteins)-29a may be a therapeutic target in SSc (show CYP11A1 Proteins).
Data indicate that mitogen-activated protein kinase (show MAPK1 Proteins) (MAPK) p38 (show MAPK1 Proteins) activation is triggered by AMP (show APRT Proteins)-activated protein kinases (AMPK (show PRKAA1 Proteins)) and mediated by TAB1 protein.
The amino acid sequence between positions 373 and 502 of TAB1 is required for TP interaction.
USP18 (show USP18 Proteins) inhibits NF-kappaB (show NFKB1 Proteins) and NFAT (show NFATC1 Proteins) activation during Th17 differentiation by deubiquitinating the TAK1 (show MAP3K7 Proteins)-TAB1 complex.
We found that endothelial TAK1 (show MAP3K7 Proteins) and TAB2 (show TAB2 Proteins), but not TAB1, were critically involved in vascular formation
TAK1 (show MAP3K7 Proteins) plays a critical role in accentuated epithelial to mesenchymal transition in obliterative bronchiolitis after lung transplantation.
data suggest a complex role of aa 452-457 of TAB1 in controlling p38 MAPK (show MAPK14 Proteins) activity and subcellular localization and implicate these residues in TAK1 (show MAP3K7 Proteins)- or p38 MAPK (show MAPK14 Proteins)-dependent post-transcriptional control of gene expression
Phosphorylation and polyubiquitination of TAK1 (show MAP3K7 Proteins) are necessary for activation of NF-kappaB (show NFKB1 Proteins) by the Kaposi's sarcoma-associated herpesvirus vGPCR.
Co-expression of TAK1 (show MAP3K7 Proteins) and TAB1 resulted in a functional and active TAK1 (show MAP3K7 Proteins)-TAB1 complex capable of directly activating full-length heterotrimeric mammalian AMP-activated protein kinase (AMPK (show PRKAA2 Proteins)) in vitro.
We confirmed that PGC (show PGC Proteins)-1b inhibited downstream inflammatory signals via binding with TAB1 and thus preventing TAB1/TAK1 (show NR2C2 Proteins) binding and TAK1 (show NR2C2 Proteins) activation.
The E3 ubiquitin ligase (show MUL1 Proteins) Itch inhibits p38alpha (show MAPK14 Proteins) signaling and skin inflammation through the ubiquitylation of Tab1.
TAB1 and TAB2 (show TAB2 Proteins) are required for activated macrophages, making TAB1 and TAB2 (show TAB2 Proteins) effective targets to control inflammation by modulating macrophage survival.
Both the MEKK1 (show MAP2K1 Proteins) PHD (show PDC Proteins) and TAB1 are critical for ES-cell differentiation
The enhanced JNK (show MAPK8 Proteins) and IkappaB kinase (show CHUK Proteins) activation in DUSP14 (show DUSP14 Proteins)-deficient T cells was attenuated by TAB1 short hairpin RNA knockdown.
TAB1 binding stabilizes active p38alpha (show MAPK14 Proteins) and induces rearrangements within the activation segment by helical extension of the Thr (show TRH Proteins)-Gly-Tyr (show TYR Proteins) motif, allowing autophosphorylation in cis (show CISH Proteins)
We found that endothelial TAK1 (show NR2C2 Proteins) and TAB2 (show TAB2 Proteins), but not TAB1, were critically involved in vascular formation
O-GlcNAcylation of TAB1 is required for full TAK1 (show NR2C2 Proteins) activation upon stimulation with IL-1 (show IL1A Proteins)/osmotic stress.
Epithelial TAK1 (show NR2C2 Proteins) activity is regulated through two unique, TAB1-dependent basal & TAB2 (show TAB2 Proteins)-mediated stimuli-dependent mechanisms.
XIAP (show XIAP Proteins)-TAB1-TAK1 (show NR2C2 Proteins) complex is dependent on NRAGE (show MAGED1 Proteins) for IKK-alpha (show CHUK Proteins)/beta phosphorylation and NF-kappaB (show NFKB1 Proteins) activation.
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.
TAK1-binding protein 1
, TGF-beta-activated kinase 1 and MAP3K7-binding protein 1
, mitogen-activated protein kinase kinase kinase 7-interacting protein 1
, transforming growth factor beta-activated kinase-binding protein 1
, TGF-beta-activated kinase 1-binding protein 1
, Tak1-binding protein 1
, beta activated kinase-1 binding protein-1
, mitogen activated protein kinase kinase kinase 7 interacting protein 1
, mitogen-activated protein kinase kinase kinase 7 interacting protein 1