Moesin, ezrin, and p205 are actin-binding proteins associated with neutrophil plasma membranes.

摘要: Actin-binding proteins in bovine neutrophil plasma membranes were identified using blot overlays with 125I-labeled F-actin. Along surface-biotinylated proteins, enriched major actin-binding polypeptides of 78, 81, and 205 kDa. Binding was specific for F-actin because G-actin did not bind. Further, unlabeled blocked the binding whereas other acidic biopolymers relatively ineffective. also specifically inhibited by myosin subfragment 1, but CapZ or gelsolin, suggesting that membrane like myosin, bind along sides actin filaments. The 78- 81-kDa as moesin ezrin, respectively, co-migration on sodium dodecyl sulfate-polyacrylamide gel electrophoresis immunoprecipitation antibodies ezrin. Although present detectable amounts neutrophils, radixin (a third closely related member this gene family) bound overlays. Experiments full-length truncated bacterial fusion localized site to extreme carboxy terminus, a highly conserved sequence. Immunofluorescence micrographs permeabilized cells cell "footprints" showed co-localization at cytoplasmic surface membrane, consistent role membrane-actin-linking protein.