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Isoform 1 has been identified as a low-affinity, high-capacity transporter that enhances the cellular uptake of cationic arginine, lysine, and ornithine, while isoform 2B mediates the transport of these same amino acids but with much higher affinity for arginine than isoform 1 [3]

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Critically, when we introduced mutations into the Fc that reduce FcRIIIa bindingwhile retaining the cysteine at position 330and co-expressed this construct with the cysteine-mutated FcRIIIa soluble domain, we failed to produce the complex despite robust expression of both components, indicating that the native interaction is essential for guiding and stabilizing the intermolecular disulfide (Supplementary Fig

(Article in Japanese) Katayama K

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