The galectin-3 carbohydrate recognition domain maintains plasma membrane phosphatidylserine required for KRAS function

Galectin-3 carbohydrate recognition domain activity is required to maintain plasma membrane phosphatidylserine, which supports KRAS plasma-membrane binding and nanoclustering.

• Why it matters: KRAS signaling depends on plasma-membrane nanoclusters, and prior work linked Gal-3 to KRAS membrane organization, but how Gal-3 preserves the needed lipid remained unclear.
• What they did: Gal-3 knockout or CRD inhibition depleted KRAS and PtdSer from the plasma membrane; adding exogenous PtdSer restored plasma-membrane PtdSer fully and partially restored KRAS binding.
• The result: Gal-3 CRD inhibition disrupted sphingomyelin/ceramide balance and impaired endocytic and recycling transport of PtdSer, SM, and EGFR, sustaining plasma-membrane lipid composition required for KRAS spatial organization.

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