ACBD3
- Known as:
- ACBD3
- Catalog number:
- 000989A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ACBD3
Related genes to: ACBD3
- Gene:
- ACBD3 NIH gene
- Name:
- acyl-CoA binding domain containing 3
- Previous symbol:
- GOLPH1, GOCAP1
- Synonyms:
- GCP60, PAP7
- Chromosome:
- 1q42.12
- Locus Type:
- gene with protein product
- Date approved:
- 2001-04-27
- Date modifiied:
- 2016-10-05
Related products to: ACBD3
Related articles to: ACBD3
- Acyl-CoA binding domain containing protein 3 (ACBD3) is a Golgi protein implicated in multiple cellular processes. However, its function in negative-strand RNA virus infection and innate immune responses remains poorly understood. Here, we identify ACBD3 as a novel positive regulator of host defense that potently inhibits vesicular stomatitis virus (VSV) replication in HeLa cells with ACBD3 overexpression or knockdown. Mechanistically, our investigation unveils a previously unknown ACBD3-TRIM21-MAVS axis. Co-immunoprecipitation combined with mass spectrometry analysis reveals that ACBD3 interacts with the E3 ubiquitin ligase TRIM21, and this interaction is crucial for stabilizing the mitochondrial antiviral-signaling protein (MAVS). During VSV infection, ACBD3 enhances TRIM21 protein levels, thereby promoting MAVS accumulation and facilitating the activation of type I interferon signaling. Collectively, our findings elucidate a novel mechanism by which ACBD3 sustains innate immunity via TRIM21 to restrict VSV replication, providing a potential therapeutic target and strategy for combating negative-strand RNA viruses. - Source: PubMed
Publication date: 2026/01/25
Hou PeiliLi YingyingYu ZhangpingLi XingyuHe HongbinWang Hongmei - (Cpn) is an obligate intracellular parasitic pathogen that replicates inside a membrane-bound vacuole termed the inclusion. This compartment is modified by chlamydial inclusion membrane proteins (Incs), which interact with host proteins to facilitate chlamydial development and pathogenicity. Among these, Cpn0308 localizes specifically to the inclusion membrane. Our previous study demonstrated that exogenously expressed Cpn0308 can interact with host protein ACBD3; here, we demonstrate this interaction during actual Cpn infection using endogenous proteins. This interplay proved critical for Cpn development, as ACBD3 knockout in HeLa cells led to significantly smaller inclusions, delayed transition from elementary bodies (EBs) to reticulate bodies (RBs), and reduced bacterial copy numbers. Mechanistically, the Cpn0308-ACBD3 interaction facilitates the recruitment of Phosphatidylinositol 4-kinase 3β (PI4KB) to the inclusion vicinity. This recruitment enhances the production and localization of Phosphatidylinositol 4-phosphate (PI4P) within Cpninfected HeLa cells. Conversely, PI4KB and PI4P levels were markedly diminished in Cpn-infected ACBD3-knockout cells, whereas their expression remained unchanged in uninfected knockout cells. Furthermore, pharmacological inhibition of PI4KB with PIK93 impaired PI4P synthesis and suppressed Cpn replication. In conclusion, we propose a mechanism wherein the Cpn inclusion membrane protein Cpn0308 engages host ACBD3 to recruit PI4KB around the inclusion, which subsequently catalyzes PI4P production, thereby promoting the development and progression of infection. - Source: PubMed
Publication date: 2026/06/04
Feng XiaonanCao Tian'aiJia XiaohuiJia ZeweiLi PingZhou YanJia Tianjun - Stroke remains the second leading cause of death and disability globally, yet the contribution of depressive disorders and psychological stress to stroke outcomes is often overlooked. Emerging evidence suggests that mitochondrial dysfunction may mediate this relationship. So this study aims to investigate the potential causal role of mental stress in exacerbating ischemic brain injury and identify mitochondrial proteins that contribute to this interaction. In the study, the chronic restraint stress (CRS) model was applied, and mice were subjected to 45 min of middle cerebral artery occlusion (MCAO) followed by 24 h or 48 h of reperfusion. Translocator protein (TSPO) antagonist PK11195 was injected intraperitoneally every day during CRS. Brain injury was determined by infarct volumes, cell apoptosis, Fas expression, release of lactate dehydrogenase (LDH), and reactive oxygen species (ROS). Protein expression was analyzed by Western blot. In SH-SY5Y cells, cell viability was assessed after oxygen-glucose deprivation/reoxygenation (OGD/R). Mitochondrial function was assessed after transfecting a TSPO overexpression vector (pLV-TSPO) or treated with PK11195. The results shown that CRS induced depressive-like behaviors and increased brain injury after stroke in association with impaired mitochondrial function. TSPO was elevated by CRS, and TSPO induced voltage-dependent anion channel (VDAC) phosphorylation through interaction with acyl-CoA binding domain containing 3 (ACBD3), which was reversed by PK11195. In SH-SY5Y cells, TSPO overexpression led to mitochondrial dysfunction, which was reversed by PK11195. In conclusion, the study supports a central role for TSPO in linking mental stress to adverse stroke outcomes and points to its potential as a therapeutic target for cerebrovascular health. - Source: PubMed
Publication date: 2025/12/01
Zhu YuequanLi FengwuElmadhoun OmarPang QiDing YuchuanGeng Xiaokun - In recent years, the poultry industry has embraced genome-wide assisted breeding techniques for broiler production, focusing primarily on single nucleotide polymorphisms (SNPs). However, the potential of genomic structural variations (SVs) in broiler traits remains largely unexplored due to cost and technology limitations. We developed a new chicken 21 K SV genotyping array and assessed its performance on 303 Wenchang chickens. Our evaluation showed a 99.20 % call rate with 57.13 % polymorphism across all microarray loci that identified SVs within the Wenchang chicken population. Genome-wide association studies (GWAS) of these SVs identified five significant variants associated with economically important traits, along with growth and development-related candidate genes including PLXAN4, ACBD3, and RNASET2. These findings demonstrate the value of SV-based approaches for improving genetic selection methods and enhancing productivity in poultry breeding programs. Our results show that high-quality 21 K SV genotyping arrays have significant potential for poultry breeding applications. - Source: PubMed
Publication date: 2025/08/05
Wang ChongWu ChulongPeng ChenChen AnhongZhang YuelangYu DongyouGu LihongWang ZhengguangZhao Pengju - Flavivirus infection involves extensive remodeling of the endoplasmic reticulum (ER), which is key to both the replication of the viral RNA genome as well as the assembly and release of new virions. However, little is known about how viral proteins and host factors cooperatively facilitate such a vast transformation of the ER, and how this influences the different steps of the viral life cycle. In this study, we screened for host proteins that were enriched in close proximity to the tick-borne encephalitis virus (TBEV) protein NS4B and found that the top candidates were coupled to trafficking between ER exit sites (ERES) and the Golgi. We characterized the role of ACBD3, one of the identified proteins, and showed that it promotes TBEV infection. Depletion of ACBD3 inhibited virus replication and resulted in abnormal transformation of the ER, leading to reduced virion release. ACBD3's proviral mechanism did not involve the recruitment of PI4PK as previously described for enteroviruses. Instead, productive TBEV infection required the full-length ACBD3, which localizes to ER-Golgi contact sites together with NS4B. We propose that NS4B and ACBD3 promote replication by coordinating the transformation of the ER, which is required for RNA replication and particle release. The transformation involves direct coupling to the Golgi which facilitates efficient virion transport. - Source: PubMed
Publication date: 2025/04/10
Yau Wai-LokPeters Marie B ARönfeldt SebastianSorin Marie NLindqvist RichardPulkkinen Lauri I ACarlson Lars-AndersÖverby Anna KLundmark Richard