5FPI

Mu2 adaptin subunit of the AP2 adaptor (C-terminal domain) complexed with Integrin alpha4 internalisation peptide QYKSILQE

5FPI の概要

• エントリーDOI: 10.2210/pdb5fpi/pdb
• 分子名称: AP-2 COMPLEX SUBUNIT MU, INTEGRIN ALPHA-4 SUBUNIT (3 entities in total)
• 機能のキーワード: endocytosis, clathrin adaptor
• 由来する生物種: RATTUS NORVEGICUS (NORWAY RAT); 詳細
• 細胞内の位置: Cell membrane : P84092
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 52053.25

構造登録者

Owen, D.J.,Evans, P.R.,Ivaska, J. (登録日: 2015-11-30, 公開日: 2016-01-20, 最終更新日: 2024-01-10)

主引用文献

De Franceschi, N.,Arjonen, A.,Elkhatib, N.,Denessiouk, K.,Wrobel, A.G.,Wilson, T.A.,Pouwels, J.,Montagnac, G.,Owen, D.J.,Ivaska, J.
Selective Integrin Endocytosis is Driven by Alpha Chain:Ap2 Interactions
Nat.Struct.Mol.Biol., 23:172-, 2016

PubMed Abstract: Integrins are heterodimeric cell-surface adhesion molecules comprising one of 18 possible α-chains and one of eight possible β-chains. They control a range of cell functions in a matrix- and ligand-specific manner. Integrins can be internalized by clathrin-mediated endocytosis (CME) through β subunit-based motifs found in all integrin heterodimers. However, whether specific integrin heterodimers can be selectively endocytosed was unknown. Here, we found that a subset of α subunits contain an evolutionarily conserved and functional YxxΦ motif directing integrins to selective internalization by the most abundant endocytic clathrin adaptor, AP2. We determined the structure of the human integrin α4-tail motif in complex with the AP2 C-μ2 subunit and confirmed the interaction by isothermal titration calorimetry. Mutagenesis of the motif impaired selective heterodimer endocytosis and attenuated integrin-mediated cell migration. We propose that integrins evolved to enable selective integrin-receptor turnover in response to changing matrix conditions.

PubMed: 26779610
DOI: 10.1038/NSMB.3161

実験手法

X-RAY DIFFRACTION (2.77 Å)