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J. Biol. Chem., Vol. 278, Issue 17, 15232-15238, April 25, 2003
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From the 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 shown that rapGAP I was bound to AF-6 comparably with SPA-1.
RapV12 was also bound to AF-6 via the N-terminal domain, and SPA-1 and
RapV12 were co-immunoprecipitated only in the presence of AF-6,
indicating that they could be brought into close proximity via AF-6 in
cells. Immunostaining analysis revealed that SPA-1 and RapV12 were
co-localized with AF-6 at the cell attachment sites. In HeLa cells
expressing SPA-1 in a tetracycline-regulatory manner, expression of
AF-6 inhibited endogenous Rap1GTP and
AF-6 Controls Integrin-mediated Cell Adhesion by Regulating
Rap1 Activation through the Specific Recruitment of Rap1GTP and
SPA-1*
,,,§
Department of Immunology and Cell Biology,
Graduate School of Medicine and § Graduate School of
Biostudies, Kyoto University, Sakyo-ku, Kyoto 606-8501, and the
¶ Department of Cell Pharmacology, Graduate School of
Medicine, Nagoya University, Nagoya, Aichi 466-8550, Japan
1
integrin-mediated cell adhesion to fibronectin in SPA-1-induced
conditions, whereas it affected neither of them in SPA-1-repressed
conditions. These results suggested that AF-6 could control
integrin-mediated cell adhesion by regulating Rap1 activation through
the recruitment of both SPA-1 and Rap1GTP via distinct domains.
*
This work was supported by a grant-in-aid for scientific
research from the Ministry of Education, Science, Culture, Sports, and
Technology of Japan.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Dept. of
Immunology and Cell Biology, Graduate School of Medicine, Kyoto
University, Sakyo, Kyoto 606-8501, Japan. Tel.: 81-75-753-4659; Fax:
81-75-753-4403; E-mail: minato@imm.med.kyoto-u.ac.jp.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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