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J Biol Chem, Vol. 274, Issue 51, 36153-36158, December 17, 1999
From the Recognition of sorting signals within the
cytoplasmic tail of membrane proteins by adaptor protein complexes is a
crucial step in membrane protein sorting. The three known adaptor
complexes, AP1, AP2, and AP3, have all been shown to recognize
tyrosine- and leucine-based sorting signals, which are the most common
sorting signals within membrane protein cytoplasmic tails. Although
tyrosine-based signals are recognized by the µ-chains of adaptor
complexes, the subunit recognizing leucine-based sorting signals is
less clear.
In this report we show by surface plasmon resonance that the two
leucine-based sorting signals within the cytoplasmic tail of the
invariant chain bind independently from each other to AP1 and AP2 but
not to AP3. We also show that both motifs can be recognized by the
µ-chains of AP1 and AP2. Moreover, by using monomeric as well as
trimeric invariant chain constructs, we show that adaptor binding does
not require trimerization of the invariant chain.
The Leucine-based Sorting Motifs in the Cytoplasmic Domain of
the Invariant Chain Are Recognized by the Clathrin Adaptors AP1 and AP2
and their Medium Chains*
§,
,,**
Center for Molecular Biology, University of
Heidelberg, 69120 Heidelberg, Germany, ¶ Institute for
Biochemistry II, University of Göttingen, 37073 Göttingen, Germany, and Department of Biology,
University of Oslo, N-0316 Oslo, Norway
*
This work was supported by German Science Foundation Grant
SFB523, by the Norwegian Cancer Society, and by European Community Grant XCT960058 (to K. v. F. and O. B.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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