DIRECT ASSOCIATION OF PP125(FAK) WITH PAXILLIN, THE FOCAL ADHESION-TARGETING MECHANISM OF PP125(FAK)

被引:233
作者
TACHIBANA, K
SATO, T
DAVIRRO, N
MORIMOTO, C
机构
[1] HARVARD UNIV, SCH MED, DANA FARBER CANC INST, DIV TUMOR IMMUNOL, BOSTON, MA 02115 USA
[2] HARVARD UNIV, SCH MED, DEPT MED, BOSTON, MA 02115 USA
关键词
D O I
10.1084/jem.182.4.1089
中图分类号
R392 [医学免疫学]; Q939.91 [免疫学];
学科分类号
100102 ;
摘要
Focal adhesion kinase (pp125(FAK)) is localized to focal adhesions and tyrosine phosphorylated by the engagement of pi integrins. However, it is unclear how pp125(FAK) is linked to integrin molecules. We demonstrate that pp125(FAK) is directly associated with paxillin, a 68-kD cytoskeleton protein. The COOH-terminal domain of pp125(FAK) spanning FAK residues 919-1042 is sufficient for paxillin binding and has vinculin-homologous amino acids, which are essential for paxillin binding. Microinjection and subsequent immunohistochemical analysis reveal that glutathione S-transferase-FAK fusion proteins, which bind to paxillin, localize to focal adhesions, whereas fusion proteins with no paxillin-binding activity do not localize to focal adhesions. These findings strongly suggest that pp125(FAK) is localized to focal adhesions by the direct association with paxillin.
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页码:1089 / 1099
页数:11
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