RETRACTED: Modification of TAK1 by O-linked N-acetylglucosamine facilitates TAK1 activation and promotes M1 macrophage polarization

Zhang, Dongmei; Xu, Zhiwei; Tao, Tao; Liu, Xiaojuan; Sun, Xiaolei; Ji, Yuhong; Han, Lijian; Qiu, Huiyuan; Zhu, Guizhou; Shen, Yongjun; Zhu, Liang; Shen, Aiguo

doi:10.1016/j.cellsig.2016.08.008

Cited by 11 publications

(9 citation statements)

References 34 publications

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“…Of note however, is that TAK1 function is regulated by mechanisms in addition to ubiquitination. For instance, the O-linked GlcNAcylation of TAB1 regulates TAK1 function in osmotic shock and IL1 signaling (26), and the calcium-calmodulin dependent kinase CaMKII phosphorylates TAK1 in Wnt signaling (27). Moreover, constituents of the TAK1 complex are modified by a large number of post-translational modifications (PTMs), with intricate consequences on TAK1 activity (3).…”

Section: Regulation Of Tak1 Function Composition Of the Tak1 Complex And Activationmentioning

confidence: 99%

Multifaceted roles of TAK1 signaling in cancer

Mukhopadhyay

Lee

2019

Oncogene

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Context-specific signaling is a prevalent theme in cancer biology wherein individual molecules and pathways can have multiple or even opposite effects depending on the tumor type. TAK1 represents a particularly notable example of such signaling diversity in cancer progression. Originally discovered as a TGF-β-activated kinase, over the years it has been shown to respond to numerous other stimuli to phosphorylate a wide range of downstream targets and elicit distinct cellular responses across cell and tissue types. Here we present a comprehensive review of TAK1 signaling and provide important therapeutic perspectives related to its function in different cancers.

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Section: Regulation Of Tak1 Function Composition Of the Tak1 Complex And Activationmentioning

confidence: 99%

Multifaceted roles of TAK1 signaling in cancer

Mukhopadhyay

Lee

2019

Oncogene

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“…Upon stimulation with IL-1 and NaCl, O-GlcNAcylation of TAK1 at S427 is required for T187/S192 phosphorylation and full activation of TAK1 in RAW264.7 cells (86). Thus, TAK1 O-GlcNAcylation has been found to activate downstream JNK and NF-κB signaling pathways and increase pro-inflammatory cytokine production, and finally facilitate M1 polarization of macrophages which is closely associated with acute inflammatory responses in RAW264.7 cells (87).…”

Section: Pro-inflammatory Role Of O-glcnacylationmentioning

confidence: 99%

O-GlcNAcylation in immunity and inflammation: An intricate system (Review)

Xie

Men

et al. 2019

Int J Mol Med

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Chronic, low-grade inflammation associated with obesity and diabetes result from the infiltration of adipose and vascular tissue by immune cells and contributes to cardiovascular complications. Despite an incomplete understanding of the mechanistic underpinnings of immune cell differentiation and inflammation, O-GlcNAcylation, the addition of O-linked N-acetylglucosamine (O-GlcNAc) to cytoplasmic, nuclear and mitochondrial proteins by the two cycling enzymes, the O-linked N-acetylglucosamine transferase (OGT) and the O-GlcNAcase (OGA), may contribute to fine-tune immunity and inflammation in both physiological and pathological conditions. Early studies have indicated that O-GlcNAcylation of proteins play a pro-inflammatory role in diabetes and insulin resistance, whereas subsequent studies have demonstrated that this post-translational modification could also be protective against acute injuries. These studies suggest that diverse types of insults result in dynamic changes to O-GlcNAcylation patterns, which fluctuate with cellular metabolism to promote or inhibit inflammation. In this review, the current understanding of O-GlcNAcylation and its adaptive modulation in immune and inflammatory responses is summarized.

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“…O -GlcNAcylation has recently emerged as a new type of PTM that positively regulates TAK1 activation. TAK1 Ser427 is modified with O -GlcNAc in response to IL-1α and osmotic stress, and the Ser-substituted mutant reduces TAK1 autophosphorylation and following activation of the downstream signaling without affecting the interaction between TAK1 and TAB1 [ 72 ]. IL-1α and osmotic stress also induce O -GlcNAcylation of TAB1 at Ser395 [ 80 ].…”

Section: Ptms Of Tak1 and Tabsmentioning

confidence: 99%

Post-Translational Modifications of the TAK1-TAB Complex

Hirata

Takahashi

Morishita

et al. 2017

IJMS

121

100

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Transforming growth factor-β (TGF-β)-activated kinase 1 (TAK1) is a member of the mitogen-activated protein kinase kinase kinase (MAPKKK) family that is activated by growth factors and cytokines such as TGF-β, IL-1β, and TNF-α, and mediates a wide range of biological processes through activation of the nuclear factor-κB (NF-κB) and the mitogen-activated protein (MAP) kinase signaling pathways. It is well established that activation status of TAK1 is tightly regulated by forming a complex with its binding partners, TAK1-binding proteins (TAB1, TAB2, and TAB3). Interestingly, recent evidence indicates the importance of post-translational modifications (PTMs) of TAK1 and TABs in the regulation of TAK1 activation. To date, a number of PTMs of TAK1 and TABs have been revealed, and these PTMs appear to fine-tune and coordinate TAK1 activities depending on the cellular context. This review therefore focuses on recent advances in the understanding of the PTMs of the TAK1-TAB complex.

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RETRACTED: Modification of TAK1 by O-linked N-acetylglucosamine facilitates TAK1 activation and promotes M1 macrophage polarization

Cited by 11 publications

References 34 publications

Multifaceted roles of TAK1 signaling in cancer

Multifaceted roles of TAK1 signaling in cancer

O-GlcNAcylation in immunity and inflammation: An intricate system (Review)

Post-Translational Modifications of the TAK1-TAB Complex

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