A Role for Acidic Residues in Di-leucine Motif-based Targeting to the Endocytic Pathway (∗)
L Pond, LA Kuhn, L Teyton, MP Schutze… - Journal of Biological …, 1995 - ASBMB
Recent reports have suggested that major histocompatibility complex class II molecules load
peptide through a specialized compartment of the endocytic pathway and are targeted to this
pathway by association with invariant chain (Iip31). Therefore we used a site-directed
mutagenesis approach to determine whether Iip31 possesses novel protein targeting
signals. Our results indicate that two di-leucine-like pairs mediate Iip31 targeting and that an
acidic amino acid residue four or five residues N-terminal to each Iip31 di-leucine-like pair is …
peptide through a specialized compartment of the endocytic pathway and are targeted to this
pathway by association with invariant chain (Iip31). Therefore we used a site-directed
mutagenesis approach to determine whether Iip31 possesses novel protein targeting
signals. Our results indicate that two di-leucine-like pairs mediate Iip31 targeting and that an
acidic amino acid residue four or five residues N-terminal to each Iip31 di-leucine-like pair is …
