Ask about this productRelated genes to: ACBD3 Blocking Peptide
- 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 Blocking Peptide
Related articles to: ACBD3 Blocking Peptide
- 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 - Lung cancer continues to be the leading cause of cancer-related deaths globally. Unraveling the regulators behind lung cancer growth and its metastatic spread, along with understanding the underlying mechanisms, is crucial for developing novel and effective therapeutic strategies. While much research has focused on identifying potential oncogenes or tumor suppressors, the roles of certain genes can vary depending on the context and may even exhibit contradictory effects. In this study, we demonstrate that acyl-CoA binding domain containing 3 (ACBD3), a Golgi resident protein, promotes primary lung cancer growth by recruiting phosphatidylinositol (PI)-4-kinase IIIβ (PI4KB) to the Golgi, thereby enhancing oncogenic secretion in chromosome 1q-amplified lung cancer cells. Conversely, in chromosome 1q-diploid lung cancer cells, ACBD3 acts as a suppressor of lung cancer metastasis by inhibiting the NOTCH signaling pathway and reducing cancer cell motility. This highlights the intricacy of cancer progression and cautions against simplistic approaches targeting individual oncogenes for cancer therapy. - Source: PubMed
Publication date: 2025/04/06
Tan XiaochaoWu ChaoBanerjee PriyamWang ShikeCardin Derrick LXu YutingCreighton Chad JRussell William K - is an obligate intracellular bacterium of eukaryotic cells characterized by a unique biphasic life cycle; its biosynthesis and replication must occur within a cytoplasmic vacuole or inclusion. Certain inclusion membrane proteins have been demonstrated to mediate the interactions between intra-inclusion chlamydial organisms and the host cell. It has been demonstrated previously that the -encoded Cpn0308 localizes to the inclusion membrane; however, its function remains unknown. In the current study, a yeast two-hybrid assay was conducted to screen Cpn0308 as a bait against a HeLa cell cDNA library, revealing its binding to the host protein acyl-coenzyme A binding domain-containing 3 (ACBD3). The interaction between Cpn0308 and ACBD3 was confirmed through co-immunoprecipitation and GST (Glutathione S-transferase) pull-down assays. The two proteins were also co-localized in HeLa cells co-expressing Cpn0308 and ACBD3, as well as in -infected cells, as observed under confocal fluorescence microscopy. Given that ACBD3 plays a crucial role in maintaining host cell lipid homeostasis and its Golgi dynamic domain is responsible for interacting with Cpn0308, we hypothesize that the Cpn0308-ACBD3 interaction may facilitate 's acquisition of host lipids, thereby benefiting chlamydial survival. This study lays a foundation for further elucidating the mechanisms of Cpn0308-mediated pathogenesis.IMPORTANCEThe biosynthesis and replication of () must occur within the cytoplasmic vacuoles or inclusions of host cells. Inclusion bodies play a crucial role in mediating the interactions between and host cells. Cpn0308 is localized to the inclusion membrane; however, its function is unknown. In this study, Cpn0308 was found to bind to host protein acyl-coenzyme A binding domain-containing 3 (ACBD3) through some standard approaches. Co-localization of the two proteins was observed in both original HeLa cells and Cpn-infected HeLa cells. ACBD3 plays a significant role in maintaining lipid homeostasis in host cells; we speculate that the Cpn0308-ACBD3 interaction may facilitate the acquisition of host lipids by , thereby enhancing chlamydial survival. - Source: PubMed
Publication date: 2024/12/26
Ma LiangJia Xiao-HuiGao ZheZhou YanCheng Yong-TingLi PingJia Tian-Jun