Tripartite motif-containing protein 23 (TRIM23)

Tripartite motif-containing protein 23 (TRIM23) is a multifunctional protein belonging to the TRIM family of RING-type E3 ubiquitin ligases, characterized by the presence of a RING finger, B-box domains, a coiled-coil region, and a unique C-terminal ADP-ribosylation factor (ARF) GTPase domain[1][3][4][7]. TRIM23 is essential for regulating protein ubiquitination and autophagic pathways, especially in antiviral defense, where it mediates Lys-27-linked auto-polyubiquitination to activate its GTPase domain and promote autophagosomal recruitment[2][4][6]. The protein plays key roles in innate immune signaling, autophagy, and intracellular vesicle trafficking between the Golgi apparatus and lysosomes[3][7]. It also participates in TBK1 kinase activation and modulation of p62/SQSTM1, facilitating selective autophagic elimination of pathogens and potentially influencing cellular responses to infections and cancer. Disease associations include immunodeficiency disorders and rare genetic syndromes, with emerging links to viral infection outcomes[3][6].

Other names

TRIM23ARD1ARFD1RNF46E3 ubiquitin-protein ligase TRIM23ADP-ribosylation factor domain-containing protein 1GTP-binding protein ARD-1RING finger protein 46RING-type E3 ubiquitin transferase TRIM23tripartite motif-containing protein 23

Targeting or modulating E3 ubiquitin-protein ligase activity; Modulation of autophagy (e.g., through TBK1 activation, p62 phosphorylation); Targeting GTPase activity or ARF domain function