ArticleThe Journal of cell biology2026
Integrins and tetraspanins mediate CD36-actin coupling and regulate CD36 organization and signaling.
Article in The Journal of cell biology, 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
1 citing paper in PubMed.
- Investigation of CD36 interactome provides insights into multimolecular complexes necessary for anti-angiogenic signalling.bioRxiv : the preprint server for biology · 2025Article
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8 authors.
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Abstract
Submembrane cortical actin (CA) plays a large role in regulating the dynamic organization of cell surface receptors, which in turn regulates receptor signaling. Many receptors have short intracellular domains and no known link to actin. Here, we identified the β1-integrin subunit and several tetraspanins (CD9, CD81, and CD151) as part of the hitherto unknown molecular link between the receptor CD36 and CA. Our data indicate that CD36 in vascular endothelial cells interacts with these proteins, with stronger interactions near the cell edge. Compromising these interactions via the point mutation G12V in the N-terminal transmembrane domain of CD36 alters the dynamic organization of CD36 on the cell surface and weakens its coupling to CA dynamics. Moreover, it abolishes thrombospondin-1-induced CD36 signaling through the Src family kinase Fyn. Given their many interactions with transmembrane proteins, tetraspanins and integrins may provide a ubiquitous mechanism for plasma membrane-CA coupling.
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