| First Author | Xu X | Year | 2014 |
| Journal | PLoS One | Volume | 9 |
| Issue | 8 | Pages | e105561 |
| PubMed ID | 25133611 | Mgi Jnum | J:219121 |
| Mgi Id | MGI:5619680 | Doi | 10.1371/journal.pone.0105561 |
| Citation | Xu X, et al. (2014) Mst1 directs Myosin IIa partitioning of low and higher affinity integrins during T cell migration. PLoS One 9(8):e105561 |
| abstractText | Chemokines promote T cell migration by transmitting signals that induce T cell polarization and integrin activation and adhesion. Mst1 kinase is a key signal mediator required for both of these processes; however, its molecular mechanism remains unclear. Here, we present a mouse model in which Mst1 function is disrupted by a hypomorphic mutation. Microscopic analysis of Mst1-deficient CD4 T cells revealed a necessary role for Mst1 in controlling the localization and activity of Myosin IIa, a molecular motor that moves along actin filaments. Using affinity specific LFA-1 antibodies, we identified a requirement for Myosin IIa-dependent contraction in the precise spatial distribution of low and higher affinity LFA-1 on the membrane of migrating T cells. Mst1 deficiency or Myosin inhibition resulted in multipolar cells, difficulties in uropod detachment and mis-localization of low affinity LFA-1. Thus, Mst1 regulates Myosin IIa dynamics to organize high and low affinity LFA-1 to the anterior and posterior membrane during T cell migration. |
