Neutrophils respond to inflammation with adhesion to endothelia, extravasation into tissues, and migration toward the site of infection or injury. Migration is dependent on the interplay of various adhesion molecules, yet integrin aMb2 play a dominant role in guiding neutrophils toward greater concentrations of chemoattractants. The precise and timely neutrophil response to a localized infection is crucial in the early phase of an immune response. Redundant mechanisms exist to ensure directed migration toward and capture of microbial pathogens. We have shown that one of the crucial responses to inflammation drives activation of peptidylarginine deiminase (PAD4) and the release of neutrophil extracellular traps (NETs). Additional contributions to the response to inflammation include the deimination of cytoskeletal substrates. These include various actin cytoskeletal regulating proteins, including profilin, drebrin-like protein, and coronin 1A. Here, we examine ezrin, which along with radixin and moesin form the ERM complex of proteins that act as cytoskeletal adaptors. The ERMs bind to cytoplasmic tails of transmembrane proteins, including Mac-1 integrins, and link them to actin filaments. Phosphatases and kinases regulate the transition between the active and inactive conformations of ERMs. Here, we examine ezrin deimination and its role in neutrophil adhesion during neutrophil swarming and directed migration.