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• W2086562923 abstract "The protein mediating system L amino acid transport, AmAT‐L, is a disulfide‐linked heterodimer of a permease‐related light chain (AmAT‐L‐lc) and the type II glycoprotein 4F2hc/CD98. The Schistosoma mansoni protein SPRM1 also heterodimerizes with h 4F2hc, inducing amino acid transport with different specificity. In this study, we show that the disulfide bond is formed by heavy chain C109 with a Cys residue located in the second putative extracellular loop of the multi‐transmembrane domain light chain (C164 and C137 for X AmAT‐L‐lc and SPRM1, respectively). The non‐covalent interaction of Cys‐mutant subunits is not sufficient to allow coimmunoprecipitation, but cell surface expression of the light chains is maintained to a large extent. The non‐covalently linked transporters display the same transport characteristics as disulfide bound heterodimers, but the maximal transport rates are reduced by 30–80%." @default.
• W2086562923 created "2016-06-24" @default.
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• W2086562923 date "1998-11-13" @default.
• W2086562923 modified "2023-10-15" @default.
• W2086562923 title "Functional heterodimeric amino acid transporters lacking cysteine residues involved in disulfide bond" @default.
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• W2086562923 doi "https://doi.org/10.1016/s0014-5793(98)01359-3" @default.
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