ARRDC3, a novel α-arrestin, modulates WSSV replication and AHPND pathogenesis in Litopeneaus vannamei DOI
Ramya Kumar, Brandon Rafael de Jesús Castillo-Corea, Shih‐Shun Lin

et al.

Fish & Shellfish Immunology, Journal Year: 2024, Volume and Issue: unknown, P. 110074 - 110074

Published: Dec. 1, 2024

Language: Английский

Association of ARRDC3 and NFIA variants with bovine congestive heart failure in feedlot cattle DOI Creative Commons
Michael P. Heaton, Gregory P. Harhay, Adam Bassett

et al.

F1000Research, Journal Year: 2024, Volume and Issue: 11, P. 385 - 385

Published: March 4, 2024

Bovine congestive heart failure (BCHF) has become increasingly prevalent among feedlot cattle in the Western Great Plains of North America with up to 7% mortality affected herds. BCHF is an untreatable complex condition involving pulmonary hypertension that culminates right ventricular and death. Genes associated have not been previously identified. Our aim was search for genomic regions this disease.

Language: Английский

Citations

6
Arrestin domain containing 3 promotes alcohol-induced liver steatosis by reducing stearoyl-CoA desaturase-1 ubiquitinated degradation DOI Creative Commons
Yin Tang, Haoxiong Zhou, Xuemei Pan

et al.

Metabolism, Journal Year: 2025, Volume and Issue: unknown, P. 156175 - 156175

Published: March 1, 2025

Language: Английский

Citations

0
ARRDC3 tyrosine phosphorylation functions as a switch to control c-Src versus WWP2 interactions and distinct scaffolding functions DOI Creative Commons
Mika Caplan,

Carolyne Bardeleben,

Kanika Dhawan

et al.

Journal of Biological Chemistry, Journal Year: 2025, Volume and Issue: unknown, P. 110270 - 110270

Published: May 1, 2025

Mammalian α-arrestins are members of the same arrestin family as ubiquitously expressed and extensively studied β-arrestins. Arrestins share common structural elements including conserved N- C-arrestin-fold domains, polar core, finger loop, C-terminal tail, all which mediate protein-protein interactions. In β-arrestins, these domains enable control G protein-coupled receptor (GPCR) signaling scaffolding interactions with various proteins c-Src. By contrast, repertoire α-arrestin partners regulatory mechanisms that their not well understood. differ considerably from β-arrestins in region; contain clathrin adaptor β-adaptin binding sites whereas harbor PPxY motifs, demonstrated to interact WW E3 ubiquitin ligases such WWP2. Here we report identification a novel phosphorylation site, tyrosine (Y) 394, embedded motif ARRDC3. The Y394 site functions phospho-regulatory switch distinct ARRDC3 functions. We found promotes interaction c-Src via its SH2 domain, non-phosphorylated form binds Our results further show domain-dependent enables regulation activity, disrupts WWP2 perturbs ARRDC3-dependent lysosomal trafficking GPCR, protease-activated receptor-1. Together findings indicate selective different impact

Language: Английский

Citations

0
E3 ubiquitin ligase WWP2 as a promising therapeutic target for diverse human diseases DOI
Shilong You, Jiaqi Xu, Yushan Guo

et al.

Molecular Aspects of Medicine, Journal Year: 2024, Volume and Issue: 96, P. 101257 - 101257

Published: March 2, 2024

Language: Английский

Citations

2
ARRDC3, a novel α-arrestin, modulates WSSV replication and AHPND pathogenesis in Litopeneaus vannamei DOI
Ramya Kumar, Brandon Rafael de Jesús Castillo-Corea, Shih‐Shun Lin

et al.

Fish & Shellfish Immunology, Journal Year: 2024, Volume and Issue: unknown, P. 110074 - 110074

Published: Dec. 1, 2024

Language: Английский

Citations

1