s-Afadin binds more preferentially to the cell adhesion molecules nectins than l-afadin.

@article{Kobayashi2014sAfadinBM,
  title={s-Afadin binds more preferentially to the cell adhesion molecules nectins than l-afadin.},
  author={Reiko Kobayashi and Souichi Kurita and Muneaki Miyata and Tomohiko Maruo and Kenji Mandai and Yoshiyuki Rikitake and Yoshimi Takai},
  journal={Genes to cells : devoted to molecular & cellular mechanisms},
  year={2014},
  volume={19 12},
  pages={853-63}
}
l-Afadin was originally purified from rat brain as an actin filament (F-actin)-binding protein that was homologous to the AF-6 gene product. Concomitantly, s-afadin that did not show an F-actin-binding capability was copurified with l-afadin. Structurally, s-afadin lacks the C-terminal F-actin-binding domain but has two short sequences that were not present in l-afadin. The properties and roles of l-afadin have intensively been investigated, but those of s-afadin have poorly been understood. We… CONTINUE READING

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