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Characterization of a γ‐adaptin ear‐binding motif in enthoprotin
Author(s) -
Wasiak Sylwia,
Denisov Alexei Yu.,
Han Zhaozhong,
Leventis Peter A.,
de Heuvel Elaine,
Boulianne Gabrielle L.,
Kay Brian K.,
Gehring Kalle,
McPherson Peter S.
Publication year - 2003
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(03)01299-7
Subject(s) - clathrin , binding site , chemistry , inner ear , alanine , vesicle , mutagenesis , biophysics , microbiology and biotechnology , biology , biochemistry , anatomy , amino acid , mutation , membrane , gene
Enthoprotin, a newly identified component of clathrin‐coated vesicles, interacts with the trans ‐Golgi network (TGN) clathrin adapters AP‐1 and GGA2. Here we perform a multi‐faceted analysis of the site in enthoprotin that is responsible for the binding to the γ‐adaptin ear (γ‐ear) domain of AP‐1. Alanine scan mutagenesis and nuclear magnetic resonance (NMR) studies reveal the full extent of the site as well as critical residues for this interaction. NMR studies of the γ‐ear in complex with a synthetic peptide from enthoprotin provide structural details of the binding site for TGN accessory proteins within the γ‐ear.