Nature Immunology
- 7, 919 - 928 (2006)
Published online: 6 August 2006; | doi:10.1038/ni1374
Spatiotemporal regulation of the kinase Mst1 by binding protein RAPL is critical for lymphocyte polarity and adhesionKoko Katagiri1, Masashi Imamura2 & Tatsuo Kinashi11
Department of Molecular Genetics, Institute of Biomedical Science, Kansai Medical University, Osaka 570-8506, Japan. 2
Center Research Institute, Ishihara Sangyo Kaisha, Kusatsu, Shiga 525-0025, Japan.
Correspondence should be addressed to Tatsuo Kinashi kinashi@takii.kmu.ac.jp 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.
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