ArticleProtein science : a publication of the Protein Society2019
Human pantothenate kinase 4 is a pseudo-pantothenate kinase.
Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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29 citing papers in PubMed, 45 citations in OpenAlex.
- Supplementation via DAF-16 andbioRxiv : the preprint server for biology · 2026Article
- Renal coenzyme A (CoA) production from VB5 fuels stem cell proliferation and tumor growth.Nature communications · 2026Article
- PANK4 Regulates YAP to Modulate the Glycolytic Pathway in LEC for Driving LECs-EMT in Early Diabetic Cataract Pathogenesis.Investigative ophthalmology & visual science · 2026Article
- Nuclear accumulation of PANK4 in hippocampal astrocytes aggravates cuproptosis in association with mild cognitive impairment in aged mice.Frontiers in aging neuroscience · 2026Article
- Pantothenate kinase 4 controls lipid synthesis for T-cell proliferation by modulating coenzyme A and glutaminolysis.Signal transduction and targeted therapy · 2025Article
- Thiazole substitution of a labile amide bond-a new option toward antiplasmodial pantothenamide-mimics.Antimicrobial agents and chemotherapy · 2025Article
- Augmented Acyl-CoA Biosynthesis Promotes Resistance to TEAD Palmitoylation Site Inhibition.ACS chemical biology · 2025Article
- Pantothenate kinase 4 controls skeletal muscle substrate metabolism.Nature communications · 2025Article
- Identification of a depupylation regulator for an essential enzyme inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Decreased PANK1 expression in kidney renal clear cell carcinoma: impact on cell apoptosis, invasion, migration, and epithelial-mesenchymal transition.Discover oncology · 2024Article
- Coenzyme A biosynthesis: mechanisms of regulation, function and disease.Nature metabolism · 2024Review
- Kinome-Wide Synthetic Lethal Screen Identifies PANK4 as a Modulator of Temozolomide Resistance in Glioblastoma.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Acetyl-CoA biosynthesis drives resistance to histone acetyltransferase inhibition.Nature chemical biology · 2023Article
- Pantothenate Kinase 4 Governs Lens Epithelial Fibrosis by Negatively Regulating Pyruvate Kinase M2-Related Glycolysis.Aging and disease · 2023Article
- Patient-Derived Cellular Models for Polytarget Precision Medicine in Pantothenate Kinase-Associated Neurodegeneration.Pharmaceuticals (Basel, Switzerland) · 2023Review
- Diagnosis and Treatment of Pantothenate Kinase-Associated Neurodegeneration (PKAN): A Systematic Review.Cureus · 2023Review
- Inherited Disorders of Coenzyme A Biosynthesis: Models, Mechanisms, and Treatments.International journal of molecular sciences · 2023Review
- Evidence for a Conserved Function of Eukaryotic Pantothenate Kinases in the Regulation of Mitochondrial Homeostasis and Oxidative Stress.International journal of molecular sciences · 2022Article
- Generation and Validation of an Anti-Human PANK3 Mouse Monoclonal Antibody.Biomolecules · 2022Article
- Never-homozygous genetic variants in healthy populations are potential recessive disease candidates.NPJ genomic medicine · 2022Article
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4 authors at 1 institution in 1 country.
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Abstract
Pantothenate kinase generates 4'-phosphopantothenate in the first and rate-determining step of coenzyme A (CoA) biosynthesis. The human genome encodes three well-characterized and nearly identical pantothenate kinases (PANK1-3) plus a putative bifunctional protein (PANK4) with a predicted amino-terminal pantothenate kinase domain fused to a carboxy-terminal phosphatase domain. Structural and phylogenetic analyses show that all active, characterized PANKs contain the key catalytic residues Glu138 and Arg207 (HsPANK3 numbering). However, all amniote PANK4s, including human PANK4, encode Glu138Val and Arg207Trp substitutions which are predicted to inactivate kinase activity. Biochemical analysis corroborates bioinformatic predictions-human PANK4 lacks pantothenate kinase activity. Introducing Glu138Val and Arg207Trp substitutions to the human PANK3 and plant PANK4 abolished their robust pantothenate kinase activity. Introducing both catalytic residues back into human PANK4 restored kinase activity, but only to a low level. This result suggests that epistatic changes to the rest of the protein already reduced the kinase activity prior to mutation of the catalytic residues in the course of evolution. The PANK4 from frog, an anamniote living relative encoding the catalytically active residues, had only a low level of kinase activity, supporting the view that HsPANK4 had reduced kinase activity prior to the catalytic residue substitutions in amniotes. Together, our data show that human PANK4 is a pseudo-pantothenate kinase-a catalytically deficient variant of the catalytically active PANK4 found in plants and fungi. The Glu138Val and Arg207Trp substitutions in amniotes (HsPANK3 numbering) completely deactivated the pantothenate kinase activity that had already been reduced by prior epistatic mutations.
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