Activation of IKK by TNFalpha requires site-specific ubiquitination of RIP1 and polyubiquitin binding by NEMO.

By Chee-Kwee Ea, L. Deng, Zong-Ping Xia, Gabriel Pineda, Zhijian J. Chen. Molecules and Cells, 2006

1,055 citations recorded by the source corpus.

Subfields: Cancer Research, Immunology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/76f9fa713cc658db7eed77b7cd946f9b4732d235

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Citations in the corpus

Involvement of linear polyubiquitylation of NEMO in NF-κB activation (2009, background): “Furthermore, in vitro GST pulldown and in vivo immunoprecipitation analyses showed that NEMO binds LUBAC through the CC2∼LZ domain, also referred to as the NUB (NEMO ubiquitin-binding) domai”
Regulation and Function of IKK and IKK-Related Kinases (2006, background): “However, it triggers RIP1-dependent binding of IKKγ and activation of the IKK complex (76, 77).”
A critical role of RICK/RIP2 polyubiquitination in Nod‐induced NF‐κB activation (2008, background): “Similarly, RIP (RIPK1), a RICK homologue, was shown to play a critical role in TNFainduced NF-kB activation through its polyubiquitination at K377 located in the IM region between the N-terminal kinase and C-terminal death domains (Ea et al, 2006; Li et al, 2006).”
Ubiquitylation in innate and adaptive immunity (2009, background): “Phosphorylation of IKK-β by TAK1 requires NEMO, which contains a unique ubiquitin-binding domai”
Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway (2006, background): “Interestingly, it has recently been shown that NEMO itself is a K63-linked polyubiquitin-binding protein and can bind ubiquitinated RIP1 (Ea et al., 2006; Wu et al., 2006a).”
Specific recognition of linear ubiquitin chains by NEMO is important for NF-kappaB activation. (2009, background): “…to as NUB (NEMO ubiquitin binding), CoZi (coil-zipper domain), or UBAN (ubiquitin binding in ABIN and NEMO proteins) (hereafter referred to as UBAN), which was thought to specifically bind to Lys63-ubiquitinated substrates (Wu et al., 2006; Ea et al., 2006; Bloor et al., 2008; Wagner et al., 2008).”
Molecular Basis of NF-κB Signaling (2013, background): “The L227P mutation may therefore change the helical folding tendency of NEMO and destabilize the NEMO dimer in the cell (2, 4, 14, 18, 27, 28, 39, 73, 108, 111, 120).”