[HTML][HTML] AF-6 controls integrin-mediated cell adhesion by regulating Rap1 activation through the specific recruitment of Rap1GTP and SPA-1
L Su, M Hattori, M Moriyama, N Murata… - Journal of Biological …, 2003 - ASBMB
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 it 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 it was …