3GC3

Crystal Structure of Arrestin2S and Clathrin

3GC3 の概要

• エントリーDOI: 10.2210/pdb3gc3/pdb
• 関連するPDBエントリー: 3GD1
• 分子名称: Beta-arrestin-1, Clathrin heavy chain 1 (3 entities in total)
• 機能のキーワード: protein-protein complex, phosphoprotein, sensory transduction, coated pit, cytoplasmic vesicle, membrane, endocytosis
• 由来する生物種: Bos taurus (cattle); 詳細
• 細胞内の位置: Cytoplasm: P17870; Cytoplasmic vesicle membrane; Peripheral membrane protein; Cytoplasmic side: P49951
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 83949.07

構造登録者

Williams, J.C.,Kang, D.S. (登録日: 2009-02-21, 公開日: 2009-08-25, 最終更新日: 2023-09-20)

主引用文献

Kang, D.S.,Kern, R.C.,Puthenveedu, M.A.,von Zastrow, M.,Williams, J.C.,Benovic, J.L.
Structure of an arrestin2-clathrin complex reveals a novel clathrin binding domain that modulates receptor trafficking.
J.Biol.Chem., 284:29860-29872, 2009

PubMed Abstract: Non-visual arrestins play a pivotal role as adaptor proteins in regulating the signaling and trafficking of multiple classes of receptors. Although arrestin interaction with clathrin, AP-2, and phosphoinositides contributes to receptor trafficking, little is known about the configuration and dynamics of these interactions. Here, we identify a novel interface between arrestin2 and clathrin through x-ray diffraction analysis. The intrinsically disordered clathrin binding box of arrestin2 interacts with a groove between blades 1 and 2 in the clathrin beta-propeller domain, whereas an 8-amino acid splice loop found solely in the long isoform of arrestin2 (arrestin2L) interacts with a binding pocket formed by blades 4 and 5 in clathrin. The apposition of the two binding sites in arrestin2L suggests that they are exclusive and may function in higher order macromolecular structures. Biochemical analysis demonstrates direct binding of clathrin to the splice loop in arrestin2L, whereas functional analysis reveals that both binding domains contribute to the receptor-dependent redistribution of arrestin2L to clathrin-coated pits. Mutagenesis studies reveal that the clathrin binding motif in the splice loop is (L/I)(2)GXL. Taken together, these data provide a framework for understanding the dynamic interactions between arrestin2 and clathrin and reveal an essential role for this interaction in arrestin-mediated endocytosis.

PubMed: 19710023
DOI: 10.1074/jbc.M109.023366

実験手法

X-RAY DIFFRACTION (2.2 Å)