ACBD4
- Known as:
- ACBD4
- Catalog number:
- 000990A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- ACBD4
Related genes to: ACBD4
- Gene:
- ACBD4 NIH gene
- Name:
- acyl-CoA binding domain containing 4
- Previous symbol:
- -
- Synonyms:
- FLJ13322
- Chromosome:
- 17q21.31
- Locus Type:
- gene with protein product
- Date approved:
- 2003-11-11
- Date modifiied:
- 2019-03-21
Related products to: ACBD4
Related articles to: ACBD4
- Motor-driven transport on microtubules is critical for distributing organelles throughout the cell. Most commonly, organelle movement is mediated by cargo adaptors, proteins on the surface of an organelle that directly recruit microtubule-based motors. An alternative mechanism called hitchhiking was recently discovered: some organelles move, not by recruiting the motors directly, but instead by using membrane contact sites (MCS) to attach to motor-driven vesicles and hitchhike along microtubules. Organelle hitchhiking is observed across fungi and animals. In filamentous fungi, nearly all peroxisomes move by hitchhiking on early endosomes (EE). In the fungus , EE-associated linker proteins PxdA and DipA are critical for establishing EE-peroxisome MCS required for peroxisome movement. Whether peroxisome-membrane proteins exist that regulate peroxisome hitchhiking on EEs is not known. Through a forward mutagenesis screen, we discovered an acyl-CoA binding (ACB) domain-containing protein AcbdA/AN1062 that localizes to peroxisomes via its tail-anchored transmembrane domain (TMD). Deleting the AcbdA gene or only its N-terminal ACB domain perturbs the movement and distribution of peroxisomes. Importantly, AcbdA is not required for the movement of EEs or for the recruitment of PxdA and DipA on EEs. Fatty acid (FA)-induced increases in peroxisome movement require AcbdA, suggesting that peroxisome hitchhiking on EEs is coupled to FA metabolism. Mutating a conserved FFAT motif, predicted to interact with the endoplasmic reticulum (ER), has no effect on peroxisome movement. Taken together, our data indicate that AcbdA is a peroxisome-membrane protein required for peroxisome hitchhiking on EEs. AcbdA's involvement in peroxisome hitchhiking represents a divergence from known functions of Acbd4/5 proteins and adds layers to our understanding of the functionality of the Acbd4/5 family of proteins. - Source: PubMed
Publication date: 2025/09/03
Driscoll Bellana EFountain Madison BGates Isabella NAbdollahi ReihaneLangley Allison MOwens Matthew BChristensen Jenna RSalogiannis John - Motor-driven transport on microtubules is critical for distributing organelles throughout the cell. Most commonly, organelle movement is mediated by cargo adaptors, proteins on the surface of an organelle that directly recruit microtubule-based motors. An alternative mechanism called hitchhiking was recently discovered: some organelles move, not by recruiting the motors directly, but instead by using membrane contact sites to attach to motor-driven vesicles and hitchhike along microtubules. Organelle hitchhiking is observed across fungi and animals. In filamentous fungi, nearly all peroxisomes move by hitchhiking on early endosomes (EEs). In the fungus , EE-associated linker proteins PxdA and DipA are critical for establishing EE-peroxisome membrane contact sites required for peroxisome movement. How peroxisomes recognize this subset of EEs and what peroxisome-membrane proteins exist that can interact with EEs is not known. Here, we undertook a forward mutagenesis screen to identify such proteins. We discovered an acyl-coA binding (ACB) domain-containing protein AcbdA/AN1062 that localizes to peroxisomes via its tail-anchored transmembrane domain (TMD). Deleting the AcbdA gene or only its N-terminal ACB domain perturbs the movement and distribution of peroxisomes. Importantly, AcbdA is not required for the movement of EEs or for the recruitment of PxdA and DipA on EEs. Fatty acid (FA)-induced increases in peroxisome movement require AcbdA, suggesting that peroxisome hitchhiking on EEs is coupled to FA metabolism. Mutating a conserved FFAT motif, predicted to interact with the endoplasmic reticulum (ER), has no effect on peroxisome movement. Taken together, our data indicate that AcbdA is a peroxisome-membrane protein required to tether peroxisomes to EEs during hitchhiking. AcbdA's involvement in peroxisome-EE contact site formation represents a divergence from known functions of Acbd4/5 proteins and adds layers to our understanding of the functionality of the Acbd4/5 family of proteins. - Source: PubMed
Publication date: 2025/04/23
Driscoll BellanaFountain Madison BGates Isabella NAbdollahi ReihaneLangley Allison MOwens Matthew BChristensen Jenna RSalogiannis John - Waterfowl fatty liver has high nutritional value and offers benefits to human health. While previous research on fatty liver has focused on individual organs, this study explored fatty liver by examining the cecum, serum metabolites, and liver gene expression. This study integrated transcriptomic, metabolomic, and 16S rRNA microbiome analyses to analyze the molecular mechanism of waterfowl fatty liver formation. We identified seven core genes, five core metabolites, and three core microorganisms, which were significantly correlated. Overfeeding increased the abundance of Mucispirillum in the cecum, while Prevotella and Olsenella decreased. These microbial shifts, mediated by metabolites such as phthalic acid, influenced lipid metabolism, which induced changes in liver gene expression, including upregulation of ACBD4 and downregulation of HSP90B1 and HSPA5, thereby supporting fatty liver development. Additionally, ABC transporters, protein processing in the endoplasmic reticulum, and amino acid metabolism were important in fatty liver development. Our research findings provide new insights into the molecular mechanism of fatty liver with overfeeding in waterfowl from the perspective of the gut-liver axis. - Source: PubMed
Publication date: 2025/06/06
Qi JingjingLi JunpengXi YangYang ZhaoGuo ShihaoHan XuWang RuiLi LiangBai LiliHan ChunchunWang JiwenLiu Hehe - The hippocampus, with its complex subfields, is linked to numerous neuropsychiatric traits. While most research has focused on its global structure or a few specific subfields, a comprehensive analysis of hippocampal substructures and their genetic correlations across a wide range of neuropsychiatric traits remains underexplored. Given the hippocampus's high heritability, considering hippocampal and subfield volumes (HASV) as endophenotypes for neuropsychiatric conditions is essential. - Source: PubMed
Publication date: 2024/10/11
Ning CaiboJin MengCai YiminFan LinyunHu KexinLu ZequnZhang MingChen CanLi YanminHu NaifanZhang DonghuiLiu YizhuoChen ShuoniJiang YuanHe ChunyiWang ZhuoCao ZilongLi HantingLi GaoyuanMa QianyingGeng HuiTian WenZhang HengYang XiaojunHuang ChaoqunWei YongchangLi BinZhu YingLi XiangpanMiao XiaopingTian Jianbo - Acyl-CoA binding domain-containing proteins (ACBDs) perform diverse but often uncharacterised functions linked to cellular lipid metabolism. Human ACBD4 and ACBD5 are closely related peroxisomal membrane proteins, involved in tethering of peroxisomes to the ER and capturing fatty acids for peroxisomal β-oxidation. ACBD5 deficiency causes neurological abnormalities including ataxia and white matter disease. Peroxisome-ER contacts depend on an ACBD4/5-FFAT motif, which interacts with ER-resident VAP proteins. As ACBD4/5-like proteins are present in most fungi and all animals, we combined phylogenetic analyses with experimental approaches to improve understanding of their evolution and functions. Notably, all vertebrates exhibit gene sequences for both ACBD4 and ACBD5, while invertebrates and fungi possess only a single ACBD4/5-like protein. Our analyses revealed alterations in domain structure and FFAT sequences, which help understanding functional diversification of ACBD4/5-like proteins. We show that the Drosophila melanogaster ACBD4/5-like protein possesses a functional FFAT motif to tether peroxisomes to the ER via Dm_Vap33. Depletion of Dm_Acbd4/5 caused peroxisome redistribution in wing neurons and reduced life expectancy. In contrast, the ACBD4/5-like protein of the filamentous fungus Ustilago maydis lacks a FFAT motif and does not interact with Um_Vap33. Loss of Um_Acbd4/5 resulted in an accumulation of peroxisomes and early endosomes at the hyphal tip. Moreover, lipid droplet numbers increased, and mitochondrial membrane potential declined, implying altered lipid homeostasis. Our findings reveal differences between tethering and metabolic functions of ACBD4/5-like proteins across evolution, improving our understanding of ACBD4/5 function in health and disease. The need for a unifying nomenclature for ACBD proteins is discussed. - Source: PubMed
Publication date: 2024/09/11
Kors SuzanSchuster MartinMaddison Daniel CKilaru SreedharSchrader Tina ACostello Joseph LIslinger MarkusSmith Gaynor ASchrader Michael