cd19773

first B-box-type 2 zinc finger found in tripartite motif-containing protein 23 (TRIM23) and similar proteins

CDD entry
Member databaseCDD
CDD typedomain
Short nameBbox2_TRIM23_C-IX_rpt1
SetBbox_SF

Description

TRIM23, also known as ADP-ribosylation factor domain-containing protein 1, GTP-binding protein ARD-1, or RING finger protein 46 (RNF46), is an E3 ubiquitin-protein ligase belonging to the C-IX subclass of TRIM (tripartite motif) family of proteins that are defined by an N-terminal RBCC (RING, Bbox, and coiled coil) domains, including three consecutive zinc-binding domains, a RING finger, two Bbox2, and a coiled coil region, as well as C-terminal ADP ribosylation factor (ARF) domains. The type 2 B-box (Bbox2) zinc finger is characterized by a CHC3H2 zinc-binding consensus motif. TRIM23 is involved in nuclear factor (NF)-kappaB activation. It mediates atypical lysine 27 (K27)-linked polyubiquitin conjugation to NF-kappaB essential modulator NEMO, also known as IKKgamma, which plays an important role in the NF-kappaB pathway, and this conjugation is essential for TLR3- and RIG-I/MDA5-mediated antiviral innate and inflammatory responses. It also regulates adipocyte differentiation via stabilization of the adipogenic activator peroxisome proliferator-activated receptor gamma (PPARgamma) through atypical ubiquitin conjugation to PPARgamma. Moreover, TRIM23 interacts with and polyubiquitinates yellow fever virus (YFV) NS5 to promote its binding to STAT2 and trigger type I interferon (IFN-I) signaling inhibition.
[3, 8, 10, 5, 1, 4, 2, 7, 6, 9, 11]

References

1.Polyubiquitin conjugation to NEMO by triparite motif protein 23 (TRIM23) is critical in antiviral defense. Arimoto K, Funami K, Saeki Y, Tanaka K, Okawa K, Takeuchi O, Akira S, Murakami Y, Shimotohno K. Proc Natl Acad Sci U S A 107, 15856-61, (2010). PMID: 20724660

2.The E3 ubiquitin ligase TRIM23 regulates adipocyte differentiation via stabilization of the adipogenic activator PPARγ. Watanabe M, Takahashi H, Saeki Y, Ozaki T, Itoh S, Suzuki M, Mizushima W, Tanaka K, Hatakeyama S. Elife 4, e05615, (2015). PMID: 25905670

3.E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation factor domain protein 1). Vichi A, Payne DM, Pacheco-Rodriguez G, Moss J, Vaughan M. Proc Natl Acad Sci U S A 102, 1945-50, (2005). PMID: 15684077

4.The interferon signaling antagonist function of yellow fever virus NS5 protein is activated by type I interferon. Laurent-Rolle M, Morrison J, Rajsbaum R, Macleod JML, Pisanelli G, Pham A, Ayllon J, Miorin L, Martinez C, tenOever BR, Garcia-Sastre A. Cell Host Microbe 16, 314-327, (2014). PMID: 25211074

5.Identification of TRIM23 as a cofactor involved in the regulation of NF-kappaB by human cytomegalovirus. Poole E, Groves I, MacDonald A, Pang Y, Alcami A, Sinclair J. J Virol 83, 3581-90, (2009). PMID: 19176615

6.Specific functional interaction of human cytohesin-1 and ADP-ribosylation factor domain protein (ARD1). Vitale N, Pacheco-Rodriguez G, Ferrans VJ, Riemenschneider W, Moss J, Vaughan M. J Biol Chem 275, 21331-9, (2000). PMID: 10748148

7.Characterization of a GTPase-activating protein that stimulates GTP hydrolysis by both ADP-ribosylation factor (ARF) and ARF-like proteins. Comparison to the ARD1 gap domain. Ding M, Vitale N, Tsai SC, Adamik R, Moss J, Vaughan M. J Biol Chem 271, 24005-9, (1996). PMID: 8798635

8.Purification and properties of ARD1, an ADP-ribosylation factor (ARF)-related protein with GTPase-activating domain. Vitale N, Moss J, Vaughan M. Methods Enzymol 329, 324-34, (2001). PMID: 11210552

9.Localization of ADP-ribosylation factor domain protein 1 (ARD1) in lysosomes and Golgi apparatus. Vitale N, Horiba K, Ferrans VJ, Moss J, Vaughan M. Proc Natl Acad Sci U S A 95, 8613-8, (1998). PMID: 9671726

10.ADP-ribosylation factor domain protein 1 (ARD1), a multifunctional protein with ubiquitin E3 ligase, GAP, and ARF domains. Vichi A, Moss J, Vaughan M. Methods Enzymol 404, 195-206, (2005). PMID: 16413270

11.ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl-terminal ADP-ribosylation factor domain. Mishima K, Tsuchiya M, Nightingale MS, Moss J, Vaughan M. J Biol Chem 268, 8801-7, (1993). PMID: 8473324

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