Characterization of a γ‐adaptin ear‐binding motif in enthoprotin

FEBS Letters

Wasiak, Sylwia¹  Leventis, Peter A.³  Gehring, Kalle²  Kay, Brian K.⁴  Boulianne, Gabrielle L.³  McPherson, Peter S.¹  Han, Zhaozhong⁴  de Heuvel, Elaine¹  Denisov, Alexei Yu.² 

[1] Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, 3801 University St., Montreal, QC, Canada H3A 2B4;Department of Biochemistry and Montreal Joint Centre for Structural Biology, McGill University, Montreal, QC, Canada H3G 1Y6;Department of Molecular and Medical Genetics, Developmental Biology Program, Hospital for Sick Children, University of Toronto, Toronto, ON, Canada M5G 1X8;Biosciences Division, Argonne National Laboratories, Argonne, IL 60439, USA

关键词: AP-1;    AP-2;    Clathrin;    Clathrin-coated vesicle;    NMR;    trans-Golgi network;   

DOI  :  10.1016/S0014-5793(03)01299-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown