Dendritic cells: Actin a dangerous part

摘要

Immunohistochemistry analyses using fixed and permeabilized fibroblasts showed that CLEC9A binding activity colocalized with F-actin, but not with all cellular actin. The authors found that CLEC9A recognizes F-actin complexed to the actin-binding domain of certain cytoskeletal molecules, including spectrin and actinin. They propose that the role of the cytoskeletal molecules is to maintain actin in a filamentous conformation, which is necessary for recognition by CLEC9A. Zhang etal. also determined the crystal structure of the C-type lectin domain of CLEC9A; these studies support the idea that CLEC9A molecules dimerize. Furthermore, their structural work identified two conserved tryptophan residues that are crucial for the recognition of F-actin by CLEC9A.