Protein targeting by tyrosine- and di-leucine-based signals: evidence for distinct saturable components

@article{Marks1996ProteinTB,
  title={Protein targeting by tyrosine- and di-leucine-based signals: evidence for distinct saturable components},
  author={Michael S Marks and Lesley Woodruff and Hiroshi Ohno and Juan S Bonifacino},
  journal={The Journal of Cell Biology},
  year={1996},
  volume={135},
  pages={341 - 354}
}
Targeting of transmembrane proteins to lysosomes, endosomal compartments, or the trans-Golgi network is largely dependent upon cytoplasmically exposed sorting signals. Among the most widely used signals are those that conform to the tyrosine-based motif, YXXO (where Y is tyrosine, X is any amino acid, and O is an amino acid with a bulky hydrophobic group), and to the di-leucine (or LL) motif. Signals conforming to both motifs have been implicated in protein localization to similar post-Golgi… CONTINUE READING
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