E3 ubiquitin-protein ligase TRIM39

Definition:

[Isoform 1]: E3 ubiquitin-protein ligase. May facilitate apoptosis by inhibiting APC/C-Cdh1-mediated poly-ubiquitination and subsequent proteasome-mediated degradation of the pro-apoptotic protein MOAP1. Regulates the G1/S transition of the cell cycle and DNA damage-induced G2 arrest by stabilizing CDKN1A/p21. Positively regulates CDKN1A/p21 stability by competing with DTL for CDKN1A/p21 binding, therefore disrupting DCX(DTL) E3 ubiquitin ligase complex-mediated CDKN1A/p21 ubiquitination and degradation.; [Isoform 2]: Regulates the G1/S transition of the cell cycle and DNA damage-induced G2 arrest by stabilizing CDKN1A/p21. Positively regulates CDKN1A/p21 stability by competing with DTL for CDKN1A/p21 binding, therefore disrupting DCX(DTL) E3 ubiquitin ligase complex-mediated CDKN1A/p21 ubiquitination and degradation. Negatively regulates the canonical NF-kappa-B signaling pathway via stabilization of CACTIN in an ubiquitination-independent manner.

References:

[1]. Nai-Jia Huang, et al. The Trim39 ubiquitin ligase inhibits APC/CCdh1-mediated degradation of the Bax activator MOAP-1. J Cell Biol. 2012 Apr 30;197(3):361-7. [Content Brief]

[2]. Lei Zhang, et al. TRIM39 regulates cell cycle progression and DNA damage responses via stabilizing p21. Proc Natl Acad Sci U S A. 2012 Dec 18;109(51):20937-42. [Content Brief]

[3]. Masanobu Suzuki, et al. TRIM39 negatively regulates the NFκB-mediated signaling pathway through stabilization of Cactin. Cell Mol Life Sci. 2016 Mar;73(5):1085-101. [Content Brief]

[4]. San San Lee, et al. TRIM39 is a MOAP-1-binding protein that stabilizes MOAP-1 through inhibition of its poly-ubiquitination process. Exp Cell Res. 2009 Apr 15;315(7):1313-25. [Content Brief]

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