E3 ubiquitin-protein ligase TTC3

Definition:

E3 ubiquitin-protein ligase which catalyzes the formation of 'Lys-48'-polyubiquitin chains. Mediates the ubiquitination and subsequent degradation of phosphorylated Akt (AKT1, AKT2 and AKT3) in the nucleus. Acts as a terminal regulator of Akt signaling after activation; its phosphorylation by Akt, which is a prerequisite for ubiquitin ligase activity, suggests the existence of a regulation mechanism required to control Akt levels after activation. Positively regulates TGFB1-induced epithelial-mesenchymal transition and myofibroblast differentiation by mediating the ubiquitination and subsequent degradation of SMURF2. Regulates neuronal differentiation by regulating actin remodeling and Golgi organization via a signaling cascade involving RHOA, CIT and ROCK. Inhibits cell proliferation.

References:

[1]. Futoshi Suizu, et al. The E3 ligase TTC3 facilitates ubiquitination and degradation of phosphorylated Akt. Dev Cell. 2009 Dec;17(6):800-10. [Content Brief]

[2]. Yueqing Gong, et al. Overexpressed TTC3 Protein Tends to be Cleaved into Fragments and Form Aggregates in the Nucleus. Neuromolecular Med. 2019 Mar;21(1):85-96. [Content Brief]

[3]. Gaia Berto, et al. The Down syndrome critical region protein TTC3 inhibits neuronal differentiation via RhoA and Citron kinase. J Cell Sci. 2007 Jun 1;120(Pt 11):1859-67. [Content Brief]

[4]. Gaia Elena Berto, et al. The DCR protein TTC3 affects differentiation and Golgi compactness in neurons through specific actin-regulating pathways. PLoS One. 2014 Apr 2;9(4):e93721. [Content Brief]

[5]. June-Hyung Kim, et al. TTC3 contributes to TGF-β1-induced epithelial-mesenchymal transition and myofibroblast differentiation, potentially through SMURF2 ubiquitylation and degradation. Cell Death Dis. 2019 Jan 29;10(2):92. [Content Brief]

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