Biochemical and Biophysical Research Communications
Regular ArticleStructural Analysis of cDNAs for Subunits of Human Mitochondrial Fatty Acid β-Oxidation Trifunctional Protein
References (0)
Cited by (94)
A review of fatty acid oxidation disorder mouse models
2024, Molecular Genetics and MetabolismDrosophila models to study causative genes for human rare intractable neurological diseases
2021, Experimental Cell ResearchCitation Excerpt :Neuron-specific dCOA7 knockdown flies exhibited a shorter life span, locomotive defects and reduced synaptic branch length of motoneurons, suggesting that loss-of-function mutation in the human COA7 gene is responsible for the phenotype of the presented patients [124]. The mitochondrial trifunctional protein (MTP) localizing to the inner mitochondrial membrane is a hetero-octamer composed of four hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase α (HADHA) and four hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase β (HADHB) [125]. MTP catalyzes the β-oxidation of fatty acids to generate acetyl-CoA.
Identification of CR43467 encoding a long non-coding RNA as a novel genetic interactant with dFIG4, a CMT-causing gene
2020, Experimental Cell ResearchCitation Excerpt :The other CR43467 knockdown line (UAS-CR43467-IR41-61) also slightly suppressed the rough eye phenotype (Fig. 8D, E, P). Hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase/enoyl-CoA hydratase beta (HADHB) is a subunit of the mitochondrial trifunctional protein (MTP) that catalyzes the beta-oxidation of fatty acids to produce acetyl-CoA [29]. Mutations in the HADHB gene induce defects in beta-oxidation that result in a MTP deficiency, which is characterized by cardiomyopathy and recurrent Leigh-like encephalopathy.
Neuron-specific knockdown of Drosophila HADHB induces a shortened lifespan, deficient locomotive ability, abnormal motor neuron terminal morphology and learning disability
2019, Experimental Cell ResearchCitation Excerpt :These results suggest that dHADHB has an important function in regulating the formation of the synapse structure at NMJ, and locomotor dysfunctions may be caused by an aberrant motor neuron presynaptic terminal morphology in third instar larvae. Since HADHB is a subunit of the mitochondrial trifunctional protein (MTP) [1], we analyzed the morphology of mitochondria at NMJs in dHADHB knockdown larvae (Fig. 5A). Mitochondria in NMJ were detected by overexpressed GFP targeted to mitochondria [23].
Thyroid Hormone Stimulation of Adult Brain Fatty Acid Oxidation
2018, Vitamins and Hormones