ArticleNature chemical biology2015
LRAT-specific domain facilitates vitamin A metabolism by domain swapping in HRASLS3.
Article in Nature chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed, 59 citations in OpenAlex.
- Epithelial remodeling and microbial dysbiosis in the lower respiratory tract of vitamin A-deficient mouse lungs.Scientific reports · 2026Article
- Retinoid dynamics in vision: from visual cycle biology to retina disease treatments.Pharmacology & therapeutics · 2025Review
- Recent Progress inInternational journal of molecular sciences · 2025Review
- Retinoic acid signaling and metabolism in heart failure.American journal of physiology. Heart and circulatory physiology · 2025Review
- Vitamin A supply in the eye and establishment of the visual cycle.Current topics in developmental biology · 2025Review
- The Absorption, Storage, and Transport of Ocular Carotenoids and Retinoids.Annual review of vision science · 2024Review
- Macroscopic inhibition of DNA damage repair pathways by targeting AP-2α with LEI110 eradicates hepatocellular carcinoma.Communications biology · 2024Article
- Identification and classification of papain-like cysteine proteinases.The Journal of biological chemistry · 2023Article
- From mouse to human: Accessing the biochemistry of vision in vivo by two-photon excitation.Progress in retinal and eye research · 2023Review
- The Amphipathic Helix in Visual Cycle Proteins: A Review.Advances in experimental medicine and biology · 2023Review
- Phospholipase A and acyltransferase 4/retinoic acid receptor responder 3 at the intersection of tumor suppression and pathogen restriction.Frontiers in immunology · 2023Review
- Defunctionalizing intracellular organelles such as mitochondria and peroxisomes with engineered phospholipase A/acyltransferases.Nature communications · 2022Article
- Dynamic lipid turnover in photoreceptors and retinal pigment epithelium throughout life.Progress in retinal and eye research · 2022Review
- Acyl-CoA:wax alcohol acyltransferase 2 modulates the cone visual cycle in mouse retina.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2022Article
- Current Knowledge on Mammalian Phospholipase AMolecules (Basel, Switzerland) · 2022Review
- Retinyl esters form lipid droplets independently of triacylglycerol and seipin.The Journal of cell biology · 2021Article
- Protein Dynamics Influence the Enzymatic Activity of Phospholipase A/Acyltransferases 3 and 4.Biochemistry · 2021Article
- Discovery and Design of Family VIII Carboxylesterases as Highly Efficient Acyltransferases.Angewandte Chemie (International ed. in English) · 2021Article
- Molecular components affecting ocular carotenoid and retinoid homeostasis.Progress in retinal and eye research · 2021Review
- The molecular aspects of absorption and metabolism of carotenoids and retinoids in vertebrates.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2020Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Cellular uptake of vitamin A, production of visual chromophore and triglyceride homeostasis in adipocytes depend on two representatives of the vertebrate N1pC/P60 protein family, lecithin:retinol acyltransferase (LRAT) and HRAS-like tumor suppressor 3 (HRASLS3). Both proteins function as lipid-metabolizing enzymes but differ in their substrate preferences and dominant catalytic activity. The mechanism of this catalytic diversity is not understood. Here, by using a gain-of-function approach, we identified a specific sequence responsible for the substrate specificity of N1pC/P60 proteins. A 2.2-Å crystal structure of the HRASLS3-LRAT chimeric enzyme in a thioester catalytic intermediate state revealed a major structural rearrangement accompanied by three-dimensional domain swapping dimerization not observed in native HRASLS proteins. Structural changes affecting the active site environment contributed to slower hydrolysis of the catalytic intermediate, supporting efficient acyl transfer. These findings reveal structural adaptation that facilitates selective catalysis and mechanism responsible for diverse substrate specificity within the LRAT-like enzyme family.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.