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Stabilization of the TAK1 adaptor proteins TAB2 and TAB3 is critical for optimal NF-kappa B activation

Harald Braun (UGent) and Jens Staal (UGent)
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Abstract
TAB2 and TAB3 bind to K63-linked polyubiquitin chains and recruit the critical kinase MAP3K7 (TAK1). The polyubiquitin-recruited TAK1/TAB2/TAB3 complex comes in close proximity with the IKK (IKK alpha/IKK beta/IKK gamma) complex, which is recruited to M1-linked polyubiquitin chains via the IKK gamma (NEMO) component. Together, the two complexes activate the NF-kappa B family of transcription factors. NF-kappa B transcription factors are critical mediators of pro-inflammatory signals and must be tightly regulated at multiple levels. Recently, it was discovered that one such point of regulation occurs at the level of TAB2 and TAB3 protein stability by the deubiquitinase USP15. Comment on:
Keywords
BINDING, epitransduction, inflammation, lysosome, proteasome, signalophagy

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Citation

Please use this url to cite or link to this publication:

MLA
Braun, Harald, and Jens Staal. “Stabilization of the TAK1 Adaptor Proteins TAB2 and TAB3 Is Critical for Optimal NF-Kappa B Activation.” FEBS JOURNAL, 2020.
APA
Braun, H., & Staal, J. (2020). Stabilization of the TAK1 adaptor proteins TAB2 and TAB3 is critical for optimal NF-kappa B activation. FEBS JOURNAL.
Chicago author-date
Braun, Harald, and Jens Staal. 2020. “Stabilization of the TAK1 Adaptor Proteins TAB2 and TAB3 Is Critical for Optimal NF-Kappa B Activation.” FEBS JOURNAL.
Chicago author-date (all authors)
Braun, Harald, and Jens Staal. 2020. “Stabilization of the TAK1 Adaptor Proteins TAB2 and TAB3 Is Critical for Optimal NF-Kappa B Activation.” FEBS JOURNAL.
Vancouver
1.
Braun H, Staal J. Stabilization of the TAK1 adaptor proteins TAB2 and TAB3 is critical for optimal NF-kappa B activation. FEBS JOURNAL. 2020.
IEEE
[1]
H. Braun and J. Staal, “Stabilization of the TAK1 adaptor proteins TAB2 and TAB3 is critical for optimal NF-kappa B activation,” FEBS JOURNAL. 2020.
@misc{8661382,
  abstract     = {TAB2 and TAB3 bind to K63-linked polyubiquitin chains and recruit the critical kinase MAP3K7 (TAK1). The polyubiquitin-recruited TAK1/TAB2/TAB3 complex comes in close proximity with the IKK (IKK alpha/IKK beta/IKK gamma) complex, which is recruited to M1-linked polyubiquitin chains via the IKK gamma (NEMO) component. Together, the two complexes activate the NF-kappa B family of transcription factors. NF-kappa B transcription factors are critical mediators of pro-inflammatory signals and must be tightly regulated at multiple levels. Recently, it was discovered that one such point of regulation occurs at the level of TAB2 and TAB3 protein stability by the deubiquitinase USP15. Comment on:},
  author       = {Braun, Harald and Staal, Jens},
  issn         = {1742-464X},
  keywords     = {BINDING,epitransduction,inflammation,lysosome,proteasome,signalophagy},
  language     = {eng},
  pages        = {4},
  series       = {FEBS JOURNAL},
  title        = {Stabilization of the TAK1 adaptor proteins TAB2 and TAB3 is critical for optimal NF-kappa B activation},
  url          = {http://dx.doi.org/10.1111/febs.15210},
  year         = {2020},
}

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