| First Author | Katagiri K | Year | 2006 |
| Journal | Nat Immunol | Volume | 7 |
| Issue | 9 | Pages | 919-28 |
| PubMed ID | 16892067 | Mgi Jnum | J:112648 |
| Mgi Id | MGI:3662967 | Doi | 10.1038/ni1374 |
| Citation | Katagiri K, et al. (2006) Spatiotemporal regulation of the kinase Mst1 by binding protein RAPL is critical for lymphocyte polarity and adhesion. Nat Immunol 7(9):919-28 |
| abstractText | RAPL, a protein that binds the small GTPase Rap1, is required for efficient immune cell trafficking. Here we have identified the kinase Mst1 as a critical effector of RAPL. RAPL regulated the localization and kinase activity of Mst1. 'Knockdown' of the gene encoding Mst1 demonstrated its requirement for the induction of both a polarized morphology and integrin LFA-1 clustering and adhesion triggered by chemokines and T cell receptor ligation. RAPL and Mst1 localized to vesicular compartments and dynamically translocated with LFA-1 to the leading edge upon Rap1 activation, suggesting a regulatory function for the RAPL-Mst1 complex in intracellular transport of LFA-1. Our study demonstrates a previously unknown function for Mst1 of relaying the Rap1-RAPL signal to induce cell polarity and adhesion of lymphocytes. |
