TRIM23
Description
The TRIM23 (tripartite motif containing 23) is a protein-coding gene located on chromosome 5.
TRIM23 is a human gene that encodes a protein belonging to the tripartite motif (TRIM) family. This protein contains three zinc-binding domains (RING, B-box type 1, and B-box type 2) and a coiled-coil region. It also belongs to the ADP ribosylation factor (ARF) family of guanine nucleotide-binding proteins. Its carboxy terminus possesses an ARF domain and a guanine nucleotide binding site, while the amino terminus harbors a GTPase activating protein domain that acts on the guanine nucleotide binding site. TRIM23 localizes to lysosomes and the Golgi apparatus, contributing to the formation and movement of intracellular transport vesicles and phospholipase D activation. Three alternatively spliced transcript variants of TRIM23 have been documented. TRIM23 interacts with TRIM31, TRIM29, and PSCD1.
TRIM23 acts as an E3 ubiquitin-protein ligase, playing a crucial role in autophagy activation during viral infection. It activates TANK-binding kinase 1 (TBK1) by promoting its dimerization and phosphorylation of the selective autophagy receptor SQSTM1. This function is achieved by TRIM23's ability to mediate 'Lys-27'-linked auto-ubiquitination of its ADP-ribosylation factor (ARF) domain, stimulating its GTPase activity and recruitment to autophagosomes.
TRIM23 is also known as ARD1, ARFD1, RNF46.
