E3 ubiquitin-protein ligase TRIM32

Definition

Has an E3 ubiquitin ligase activity. Ubiquitinates DTNBP1 (dysbindin) and promotes its degradation. May ubiquitinate BBS2. Ubiquitinates PIAS4/PIASY and promotes its degradation in keratinocytes treated with UVB and TNF-alpha (By similarity). Also acts as a regulator of autophagy by mediating formation of unanchored 'Lys-63'-linked polyubiquitin chains that activate ULK1: interaction with AMBRA1 is required for ULK1 activation.; (Microbial infection) May play a significant role in mediating the biological activity of the HIV-1 Tat protein in vivo. Binds specifically to the activation domain of HIV-1 Tat and can also interact with the HIV-2 and EIAV Tat proteins in vivo.

References:

[1]. Matthew Locke, et al. TRIM32 is an E3 ubiquitin ligase for dysbindin. Hum Mol Genet. 2009 Jul 1;18(13):2344-58. [Content Brief]

[2]. M Di Rienzo, et al. Autophagy induction in atrophic muscle cells requires ULK1 activation by TRIM32 through unanchored K63-linked polyubiquitin chains. Sci Adv. 2019 May 8;5(5):eaau8857. [Content Brief]

[3]. R A Fridell, et al. Identification of a novel human zinc finger protein that specifically interacts with the activation domain of lentiviral Tat proteins. Virology. 1995 Jun 1;209(2):347-57. [Content Brief]

[4]. Qihong Zhang, et al. Intrinsic protein-protein interaction-mediated and chaperonin-assisted sequential assembly of stable bardet-biedl syndrome protein complex, the BBSome. J Biol Chem. 2012 Jun 8;287(24):20625-35. [Content Brief]

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