Abstract:
: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.
journal_name
J Cell Scijournal_title
Journal of cell scienceauthors
Singh RK,Liao W,Tracey-White D,Recchi C,Tolmachova T,Rankin SM,Hume AN,Seabra MCdoi
10.1242/jcs.100438subject
Has Abstractpub_date
2012-04-01 00:00:00pages
1652-6issue
Pt 7eissn
0021-9533issn
1477-9137pii
jcs.100438journal_volume
125pub_type
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