| First Author | Singh RK | Year | 2012 |
| Journal | J Cell Sci | Volume | 125 |
| Issue | Pt 7 | Pages | 1652-6 |
| PubMed ID | 22375060 | Mgi Jnum | J:197700 |
| Mgi Id | MGI:5494354 | Doi | 10.1242/jcs.100438 |
| Citation | Singh RK, et al. (2012) Rab27a-mediated protease release regulates neutrophil recruitment by allowing uropod detachment. J Cell Sci 125(Pt 7):1652-6 |
| abstractText | Neutrophil migration is vital for immunity and precedes effector functions such as pathogen killing. Here, we report that this process is regulated by the Rab27a GTPase, a protein known to control granule exocytosis. Rab27a-deficient (Rab27a KO) neutrophils exhibit migration defects in vitro and in vivo, and live-cell microscopy suggests that delayed uropod detachment causes the migratory defect. Surface expression of CD11b, a key adhesion molecule, is increased in chemokine-stimulated Rab27a KO neutrophils compared with the control, suggesting a turnover delay caused by a defect in elastase secretion from azurophilic granules at the rear of bone marrow polymorphonuclear leukocytes (BM-PMNs). We suggest that Rab27a-dependent protease secretion regulates neutrophil migration through proteolysis-dependent de-adhesion of uropods, a mechanism that could be conserved in cell migration and invasion. |
