Beta-catenin migrates to the nucleus

Stable Identifier
R-HSA-3134914
Type
Reaction [omitted]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
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Phosphorylated β-catenin migrates to the nucleus where it functions as a coactivator of IRF3-dependent transcription (Yang P et al. 2010). Besides phosphorylation, other post-translational modifications of β-catenin including O-GlcNAc-glycosylation (Ha JR et al., 2014) or acetylation (reviewed by You H et al., 2022) may regulate stability, subcellular localization and function of β-catenin.

The mechanisms that control β-catenin localization are not fully elucidated. β-catenin transport to the nucleus is thought to occur in a NLS (nuclear localization signal)- and importin-independent manner through direct interaction with the nuclear pore complex (NPC) components. This has been shown to be the case for Wnt-signaling in mammalian cells (Yokoya F et al. 1999; Koike M et al. 2004). β-catenin may also 'piggy-back' into the nucleus in complex with other proteins such as FOXM1 (Zhang N et al., 2011 ) or BCL9 (Townsley FM et al., 2004).

Literature References
PubMed ID Title Journal Year
15173161 beta-Catenin shows an overlapping sequence requirement but distinct molecular interactions for its bidirectional passage through nuclear pores

Taniguchi, N, Imamoto, N, Koike, M, Furuta, M, Yokoya, F, Kose, S, Yoneda, Y

J. Biol. Chem. 2004
20453844 The cytosolic nucleic acid sensor LRRFIP1 mediates the production of type I interferon via a beta-catenin-dependent pathway

Wen, M, Rui, Y, Liu, X, Yang, P, Cao, X, Zheng, Y, An, H

Nat. Immunol. 2010
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