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Human TGF-beta Activated Kinase 1/MAP3K7 Binding Protein 1 (TAB1) interaction partners

1. the present results indicated that miR889 inhibits the aggressive behaviors of nonsmall cell lung cancer (NSCLC) by directly targeting TAB1 mRNA, thus highlighting the importance of the miR889/TAB1 pathway in the malignant progression of NSCLC.

2. multiple GPCR agonists utilize non-canonical TAB1-TAB2 and TAB1-TAB3-dependent p38 activation to promote endothelial inflammatory responses.

3. Silencing of TAB1, but not TAK1, prevented p38MAPK activation, which is indicative of TAB1-mediated autophosphorylation of p38MAPK

4. Based on the crystal structure of the p38alpha-TAB1 complex authors replaced threonine 185 of p38alpha with glycine (T185G) to prevent an intramolecular hydrogen bond with Asp150 from being formed. This mutation did not interfere with TAB1 binding to p38alpha.

5. High TAB1 expression is associated with colorectal cancer.

6. TAB1 was identified as a functional target of miR-134, and the expression of TAB1 was increased by the transcription factors of NF-kappaB1, c-Rel, and ELK1 via miR-134.

7. we show that IL-1 induces robust p38a activation both in the nucleus and in the cytoplasm/membrane.Following stimulation, p38a activity returns to a basal level in absence of receptor degradation. While nuclear pulse is controlled by MKP1 through a negative feedback to pp38, its basal activity is controlled by both TAB1 and MKP1 through a positive feedback loop.

8. TAK1/TAB1 expression in non-small cell lung carcinoma tissue is significantly increased and closely associated with patient clinical prognosis.

9. miR-29a repressed TAB1-mediated TIMP-1 production in dermal fibroblasts, demonstrating that miR-29a may be a therapeutic target in SSc.

10. Data indicate that mitogen-activated protein kinase (MAPK) p38 activation is triggered by AMP-activated protein kinases (AMPK) and mediated by TAB1 protein.

11. The amino acid sequence between positions 373 and 502 of TAB1 is required for TP interaction.

12. USP18 inhibits NF-kappaB and NFAT activation during Th17 differentiation by deubiquitinating the TAK1-TAB1 complex.

13. We found that endothelial TAK1 and TAB2, but not TAB1, were critically involved in vascular formation

14. TAK1 plays a critical role in accentuated epithelial to mesenchymal transition in obliterative bronchiolitis after lung transplantation.

15. 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

16. Phosphorylation and polyubiquitination of TAK1 are necessary for activation of NF-kappaB by the Kaposi's sarcoma-associated herpesvirus vGPCR.

17. Co-expression of TAK1 and TAB1 resulted in a functional and active TAK1-TAB1 complex capable of directly activating full-length heterotrimeric mammalian AMP-activated protein kinase (AMPK) in vitro.

18. interaction with p38alpha leads to autophosphorylation and activation of p38alpha

19. The TAK1-TAB1 fusion protein is a novel constitutively active mitogen-activated protein kinase kinase kinase that stimulates AP-1 and NF-kappaB signaling pathways

20. TauAlphaBeta1beta is involved in regulating p38alpha activity in physiological conditions

Mouse (Murine) TGF-beta Activated Kinase 1/MAP3K7 Binding Protein 1 (TAB1) interaction partners

1. Study using knock-in mouse model elucidated the role of the p38alpha-TAB1 interaction during myocardial ischemia in vivo suggested that persistent p38alpha activation may be the result of the disinhibition of MAP2K3 access in the absence of TAB1 docking on p38alpha and proposed that TAB1 phosphorylation downstream of p38alpha is associated with cardiac damage during ischemia.

2. our study uncovers that RNF114-mediated ubiquitination and degradation of TAB1 activate the NF-kappaB pathway during MZT, and thus directly link maternal clearance to early embryo development.

3. We confirmed that PGC-1b inhibited downstream inflammatory signals via binding with TAB1 and thus preventing TAB1/TAK1 binding and TAK1 activation.

4. The E3 ubiquitin ligase Itch inhibits p38alpha signaling and skin inflammation through the ubiquitylation of Tab1.

5. TAB1 and TAB2 are required for activated macrophages, making TAB1 and TAB2 effective targets to control inflammation by modulating macrophage survival.

6. Both the MEKK1 PHD and TAB1 are critical for ES-cell differentiation

7. The enhanced JNK and IkappaB kinase activation in DUSP14-deficient T cells was attenuated by TAB1 short hairpin RNA knockdown.

8. TAB1 binding stabilizes active p38alpha and induces rearrangements within the activation segment by helical extension of the Thr-Gly-Tyr motif, allowing autophosphorylation in cis

9. We found that endothelial TAK1 and TAB2, but not TAB1, were critically involved in vascular formation

10. O-GlcNAcylation of TAB1 is required for full TAK1 activation upon stimulation with IL-1/osmotic stress.

11. Epithelial TAK1 activity is regulated through two unique, TAB1-dependent basal & TAB2-mediated stimuli-dependent mechanisms.

12. XIAP-TAB1-TAK1 complex is dependent on NRAGE for IKK-alpha/beta phosphorylation and NF-kappaB activation.

13. Co-expression of TAK1 and TAB1 resulted in a functional and active TAK1-TAB1 complex capable of directly activating full-length heterotrimeric mammalian AMP-activated protein kinase (AMPK) in vitro.

14. TAB1 plays an important role in mammalian embryogenesis and is required for TAK1 activation in TGF-beta signaling

15. We propose that TAB1 promotes nitric oxide-induced p38 autophosphorylation. In addition, nitric oxide-induced p38 activation seems to promote JNK inhibition and ERK activation, but this effect appears to not require TAB1.

16. TAB1alpha, but not TAB1beta, plays an important role in the activation of p38 in insulin-producing cells and therefore also in cytokine-induced beta-cell death.

17. another MAP3K (MAPK kinase kinase) may mediate the IL-1/TNFalpha-induced activation of these signalling pathways in TAB1(-/-) and MEKK3(-/-) MEFs

18. a TAB1:TAK1:IKK beta:NF-kappaB signaling axis forms aberrantly in breast cancer cells and, consequently, enables oncogenic signaling by TGF-beta

19. Cell shrinkage under the osmotic stress condition increases the concentration of TAB1-TAK1 and may oligomerize and activate TAK1 in a TAB1-dependent manner.

20. p38 was inactivated upon infection in a Leishmania surface protease Leishmania surface protease GP63 protein degradation-dependent manner, which likely involves cleavage of the upstream adaptor TAB1.