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J Biol Chem, Vol. 273, Issue 15, 8638-8645, April 10, 1998

A Region from the Medium Chain Adaptor Subunit (µ) Recognizes Leucine- and Tyrosine-based Sorting Signals

Toril BremnesDagger , Vigdis Lauvrak§, Bjørn Lindqvist§, and Oddmund BakkeDagger

From the Dagger  Department of Molecular Cell Biology, Division of Biology, University of Oslo, 0316 Oslo, Norway and the § Biotechnology Center, 0371 Oslo, Norway

Tyrosine-based sorting signals in the cytosolic tails of membrane proteins have been found to bind directly to the medium chain subunit (µ) of the adaptor complexes AP-1 and AP-2. For the leucine-based signals, an interaction with AP-1 and AP-2 has been reported, but no specific interacting subunit has been demonstrated. After searching for molecules interacting with the leucine-based sorting signals within the cytosolic tail of the major histocompatibility complex class II-associated invariant chain using a phage display approach, we identified phage clones with homology to a conserved region of the AP-1 and AP-2 µ chains. To investigate the relevance of these findings, we have expressed regions of mouse µ1 and µ2 chains on phage gene product III and investigated the binding to tail sequences from various transmembrane proteins with known endosomal targeting signals. Enzyme-linked immunosorbent binding assays showed that these phages specifically recognized peptides containing functional leucine- and tyrosine-based sorting signals, suggesting that these regions of the µ1 and µ2 chains interact with both types of sorting signals.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.


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