ArticleNature communications2025
Structure and transport mechanism of human riboflavin transporters.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Retbindin Dynamically Redistributes to Preserve Retinal Flavin-Dependent Homeostasis in Response to Riboflavin Availability and Circadian Demand.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Synergistic Promotion of Somatic Embryogenesis inPlants (Basel, Switzerland) · 2026Article
- Structural basis of glucosinolate recognition and transport by plant GTR1.Cell discovery · 2026Article
- Acquired Multiple Acyl-Coenzyme A Dehydrogenase Deficiency Associated With Sertraline in Sweden-A Nationwide Population-Based Study.European journal of neurology · 2026Article
- Pathogenesis and therapeutic strategies in the interaction between gut microbiota and enterohemorrhagic Escherichia coli infection.FEMS microbiology reviews · 2026Review
- The SLC-ome of membrane transport: From molecular discovery to physiology and clinical applications.Physiological reviews · 2025Review
Corrections and comments
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Authors and funding
13 authors.
Funding
Abstract
Riboflavin (vitamin B2) is the precursor of flavin mononucleotide (FMN) and flavin adenine dinucleotide (FAD), which act as key cofactors of many enzymes, thus has essential roles in cell growth and functions. Animals cannot synthesize riboflavin in situ, the intake, distribution and metabolism of which are mediated by three riboflavin transporters (RFVT1-3). Many mutations in RFVTs cause severe consequences. How RFVTs recognize and transport riboflavin remains largely unknown. Here we describe the cryo-electron microscopy structures of human RFVT2 and RFVT3 in complex with riboflavin in outward-occluded and inward-open states, respectively. Riboflavin is recognized by a conserved binding pocket in the central cavity of RFVTs, whereas two acidic residues in RFVT3 determine its pH-dependent activity. By combining the structural, computational and functional analyses, this study demonstrates the structural basis of riboflavin recognition and provides a structural framework for the mechanistic comprehension of riboflavin recognition, transport, and pathology in human RFVTs.
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