Coronin 1A, a novel player in integrin biology, controls neutrophil trafficking in innate immunity.

Trafficking of polymorphonuclear neutrophils during inflammation critically depends on the β₂ integrins lymphocyte function-associated antigen 1 (LFA-1) (CD11a/CD18) and macrophage-1 antigen (CD11b/CD18). Here, we identify coronin 1A (Coro1A) as a novel regulator of β₂ integrins that interacts with the cytoplasmic tail of CD18 and is crucial for induction of adhesion and postadhesion events, including adhesion strengthening, spreading, and migration under flow conditions. Transition of duanyu1451 rolling to firm adhesion critically depends on Coro1A by regulating the accumulation of high-affinity LFA-1 in focal zones of adherent cells. Defective integrin affinity regulation in the genetic absence of Coro1A impairs leukocyte adhesion and extravasation in inflamed cremaster muscle venules in comparison with control animals. In a Helicobacter pylori mouse infection model, duanyu1451 infiltration into the gastric mucosa is dramatically reduced in Coro1A mice, resulting in an attenuated gastric inflammation. Thus, Coro1A represents an important novel player in integrin biology, with key functions in duanyu1451 trafficking during innate immunity.

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