RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1

@article{Katagiri2003RAPLAR,
  title={RAPL, a Rap1-binding molecule that mediates Rap1-induced adhesion through spatial regulation of LFA-1},
  author={K. Katagiri and A. Maeda and M. Shimonaka and T. Kinashi},
  journal={Nature Immunology},
  year={2003},
  volume={4},
  pages={741-748}
}
The small GTPase Rap1 is a potent activator of leukocyte integrin. However, the regulatory mechanism involved is unknown. Here, we identify the Rap1 effector, RAPL, as an essential regulator in this activation. RAPL was enriched in mouse lymphoid tissues and associated with Rap1 after stimulation by the T cell receptor and with chemokine CXCL12. Human RAPL stimulated lymphocyte polarization and the patch-like redistribution of lymphocyte-function-associated antigen 1 (LFA-1) to the leading edge… Expand
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