恩托普洛汀中γ-衔接蛋白耳结合基序的表征

Characterization of a gamma-adaptin ear-binding motif in enthoprotin.

作者信息

Wasiak Sylwia, Denisov Alexei Yu, Han Zhaozhong, Leventis Peter A, de Heuvel Elaine, Boulianne Gabrielle L, Kay Brian K, Gehring Kalle, McPherson Peter S

机构信息

Department of Neurology and Neurosurgery, Montreal Neurological Institute, McGill University, 3801 University St., Montreal, QC, Canada H3A 2B4.

出版信息

FEBS Lett. 2003 Dec 18;555(3):437-42. doi: 10.1016/s0014-5793(03)01299-7.

DOI:10.1016/s0014-5793(03)01299-7

PMID:14675752

Abstract

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 gamma-adaptin ear (gamma-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 gamma-ear in complex with a synthetic peptide from enthoprotin provide structural details of the binding site for TGN accessory proteins within the gamma-ear.

摘要

内吞蛋白是网格蛋白包被小泡新发现的一种成分，它与反式高尔基体网络（TGN）的网格蛋白衔接蛋白AP-1和GGA2相互作用。在此，我们对内吞蛋白中负责与AP-1的γ-衔接蛋白耳（γ-耳）结构域结合的位点进行了多方面分析。丙氨酸扫描诱变和核磁共振（NMR）研究揭示了该位点的全貌以及此相互作用的关键残基。γ-耳与内吞蛋白合成肽复合物的NMR研究提供了γ-耳内TGN辅助蛋白结合位点的结构细节。