AF-6 controls integrin-mediated cell adhesion by regulating Rap1 activation through the specific recruitment of Rap1GTP and SPA-1.

@article{Su2003AF6CI,
  title={AF-6 controls integrin-mediated cell adhesion by regulating Rap1 activation through the specific recruitment of Rap1GTP and SPA-1.},
  author={Li Su and Masakazu Hattori and Masaki Moriyama and Norihito Murata and Masashi Harazaki and Kozo Kaibuchi and Nagahiro Minato},
  journal={The Journal of biological chemistry},
  year={2003},
  volume={278 17},
  pages={15232-8}
}
In the present study, we showed that SPA-1, a Rap1 GTPase-activating protein (GAP), was bound to a cytoskeleton-anchoring protein AF-6. SPA-1 and AF-6 were co-immunoprecipitated in the 293T cells transfected with both cDNAs as well as in normal thymocytes. In vitro binding studies using truncated fragments and their mutants suggested that SPA-1 was bound to the PDZ domain of AF-6 via probable internal PDZ ligand motif within the GAP-related domain. The motif was conserved among Rap1 GAPs, and… CONTINUE READING

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