ArticleJournal of advanced research2026
Unique molecular architecture of N-glycosylated TM4SF5 dimer highlights evolutionary and structural divergence among small four-transmembrane protein families.
Article in Journal of advanced research, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Repurposing niclosamide to mitigate inflammaging: a review of multi-target mechanisms in cellular senescence and age-related decline.Inflammation research : official journal of the European Histamine Research Society ... [et al.] · 2026Review
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Authors and funding
15 authors.
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No grant is acknowledged in the PubMed record.
Abstract
introductionMembrane proteins, including small four-transmembrane proteins, play roles in membrane organization and signal transduction. Generally, they share capacities for protein-protein association and subcellular translocation to regulate cellular functions.
objectivesDespite known commonalities and differences in structure and function, the relationships among the tetraspanin, CD20-like, golgi 4-transmembrane spanning transporter (Mtp), and transmembrane 4 L six (L6) families remain unclear.
methodsHere, we mostly compared TM4SF5, a transmembrane 4 L6 family member, to the genuine tetraspanins and the CD20-like family, exploring unique aspects that evolved from the small four-transmembrane proteins.
resultsTM4SF5 and other L6 membrane proteins have two conserved cysteines, affecting N-glycosylation in the large extracellular loop (LEL) and favoring a dimeric state, whereas the tetraspanins maintained their cysteine residues in addition to the CCG motif. However, TM4SF5 and other L6 membrane proteins have more sequence similarity to proteins in the CD20-like family, which lack these features in the LEL. Uniquely, TM4SF5 and other L6 membrane proteins have a β-sheet configuration in the LEL, unlike other small four-transmembrane proteins with α-helices.
conclusionTherefore, the unique features in the LEL and the N-glycosylation of TM4SF5 may contribute to dimer formation and cholesterol binding, potentially influencing regulatory roles in liver malignancy development.
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