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The μ2 Subunit of the Clathrin Adaptor AP‐2 Binds to FDNPVY and YppØ Sorting Signals at Distinct Sites
Author(s) -
Boll Werner,
Rapoport Iris,
Brunner Christian,
Modis Yorgo,
Prehn Siegfried,
Kirchhausen Tomas
Publication year - 2002
Publication title -
traffic
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.677
H-Index - 130
eISSN - 1600-0854
pISSN - 1398-9219
DOI - 10.1034/j.1600-0854.2002.30808.x
Subject(s) - clathrin , endocytic cycle , biology , internalization , microbiology and biotechnology , protein subunit , protein targeting , signal peptide , tyrosine , ldl receptor , signal transducing adaptor protein , receptor , endosome , endocytosis , biochemistry , signal transduction , peptide sequence , lipoprotein , membrane protein , membrane , gene , cholesterol
The endocytic sorting signal on the low‐density lipoprotein receptor for clathrin‐mediated internalization is the sequence FDNPVY in the receptor's cytosolic tail. We have used a combination of surface plasmon resonance and crosslinking with a photoactivated peptide probe to demonstrate the interaction between FDNPVY‐containing peptides and the μ2 chain of purified AP‐2 clathrin adaptors (the complexes responsible for plasma membrane sorting). We show that recognition of the FDNPVY signal is mediated by a binding site in the μ2‐subunit that is distinct from the site for the more general YppØ sorting signal, another tyrosine‐based sequence also recognized by μ2‐adaptin. These results suggest the possibility that low‐density lipoprotein receptor uptake may be modulated specifically and independently of other proteins in the clathrin pathway.