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• W1980219322 endingPage "29015" @default.
• W1980219322 startingPage "29009" @default.
• W1980219322 abstract "Many integral membrane proteins contain tyrosine-based signals within their cytoplasmic domains that mediate internalization from the cell surface and targeting to lysosomal compartments. Internalization depends on an interaction of the tyrosine-based signals with the clathrin-associated adaptor complex AP-2 at the plasma membrane, whereas lysosomal targeting involves interaction of the signals with an analogous complex, AP-1, at the <i>trans</i>-Golgi network. Recent studies have identified the medium chains μ₂ of AP-2 and μ₁ of AP-1 as the recognition molecules for tyrosine-based signals. We have now investigated the structural determinants for interaction of the signals with μ₂ and μ₁. The position of the signals was found to be an important determinant of interactions with μ₂ and μ₁; signals were most effective when present at the carboxyl terminus of a polypeptide sequence. Another important determinant of interactions was the identity of residues surrounding the critical tyrosine residue. Mutation of some residues affected interactions with μ₂ and μ₁ similarly, whereas other mutations had differential effects. These observations suggest that both the position and the exact sequence of tyrosine-based sorting signals are major determinants of selectivity in their interaction with clathrin-associated adaptor complexes." @default.
• W1980219322 created "2016-06-24" @default.
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• W1980219322 date "1996-11-01" @default.
• W1980219322 modified "2023-10-11" @default.
• W1980219322 title "Structural Determinants of Interaction of Tyrosine-based Sorting Signals with the Adaptor Medium Chains" @default.
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• W1980219322 doi "https://doi.org/10.1074/jbc.271.46.29009" @default.
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