Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2

@article{Franceschi2016SelectiveIE,
  title={Selective integrin endocytosis is driven by interactions between the integrin α-chain and AP2},
  author={Nicola De Franceschi and Antti Arjonen and Nadia Elkhatib and Konstantin A. Denessiouk and Antoni G Wrobel and Thomas A Wilson and Jeroen Pouwels and Guillaume Montagnac and David R. Owen and Johanna Ivaska},
  journal={Nature Structural &Molecular Biology},
  year={2016},
  volume={23},
  pages={172-179}
}
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… CONTINUE READING