CK2 phosphorylates NFE2L2

Stable Identifier
R-HSA-8932322
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
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Upon stimulation by oxidative/electrophilic stress, Nuclear factor erythroid 2-related NFE2L2 (NRF2) is phosphorylated at the transcription activation domain (TA) by Casein kinase 2 (CK2). Deletional analysis revealed the transcription activation domains Neh4 (Nrf2-ECH homology 4) and Neh5 (Nrf2-ECH homology 5) as a major region necessary for the phosphorylation. The phosphorylation of these sites correlates with the NFE2L2 release and translocation into the nucleus and this translocation is reduced in the presence of a CK2 inhibitor (Apopa et al. 2008, Pi et al. 2007).

Literature References
PubMed ID Title Journal Year
17512459 Molecular mechanism of human Nrf2 activation and degradation: role of sequential phosphorylation by protein kinase CK2

Pi, J, Bai, Y, Reece, JM, Williams, J, Liu, D, Freeman, ML, Fahl, WE, Shugar, D, Liu, J, Qu, W, Collins, S, Waalkes, MP

Free Radic. Biol. Med. 2007
18273910 Phosphorylation of Nrf2 in the transcription activation domain by casein kinase 2 (CK2) is critical for the nuclear translocation and transcription activation function of Nrf2 in IMR-32 neuroblastoma cells

Apopa, PL, He, X, Ma, Q

J. Biochem. Mol. Toxicol. 2008
Participants
Participates
Catalyst Activity

protein serine/threonine kinase activity of Casein kinase II [cytosol]

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Regulator
Summation

Excess accumulation of reactive oxygen species in the cilium can result in the misfolding of cilia proteins leading to shortening of the cilia (Lam HC et al. 2013, Kim JI et al. 2013).

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