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It preferentially transports branched AAs, and their substrates including Phe, Trp, Leu, Ile, Met, His, Tyr, Val and Thr, most of which are essential AA
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It has been then shown that -synuclein, similarly to several aggregation-prone proteins that directly contribute to neurodegeneration are modified by a specific O -glycan, the O -GlcNAcylation ( O -GlcNAcylation has been shown to affect the phosphorylation of -synuclein and block the toxicity of -synuclein, suggesting that increasing O -GlcNAcylation may prevent protein aggregation (Marotta et al., 2015) ( Figure 4 )
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