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(Received for publication, June 25, 1996, and in revised form, September 6, 1996)
From the Cell Biology and Metabolism Branch, 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
trans-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.
Volume 271, Number 46,
Issue of November 15, 1996
pp. 29009-29015
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
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