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J Biol Chem, Vol. 274, Issue 1, 11-19, January 1, 1999
1 Cytoplasmic
Domain with ICAP-1 Protein
From the Dana-Farber Cancer Institute and Department of Pathology,
Harvard Medical School, Boston, Massachusetts 02115
In a yeast two-hybrid screen, a protein named
ICAP-1 (
1 integrin cytoplasmic domain associated
protein) associated with the integrin 1 cytoplasmic tail
but not with tails from three other integrin subunits
(2, 3, and 5) or from
seven different 
subunits. Likewise in human cells, ICAP-1
associated specifically with the 1 but not
2, 3, or 5 tails. The
carboxyl-terminal 14 amino acids of 1 were critical for
ICAP-1 interaction. ICAP-1 is a ubiquitously expressed protein of 27 and 31 kDa, with the smaller form being preferentially solubilized by
Triton X-100. Phosphorylation of both 27- and 31-kDa forms was
constitutive but was increased by 1.5-2-fold upon cell spreading on
fibronectin, compared with poly-L-lysine. Also, ICAP-1
contributes to 1 integrin-dependent migration because (i) ICAP-1 transfection markedly increased
chemotactic migration of COS7 cells through fibronectin-coated but not
vitronectin-coated porous filters, and (ii) support of
1-dependent cell migration (in Chinese
hamster ovary cells transfected with various wild type and mutant
1 forms) correlated with ICAP-1 association. In summary,
ICAP-1 (i) associates specifically with 1 integrins, (ii) is phosphorylated upon 1 integrin-mediated
adhesion, and (iii) may regulate 1-dependent cell migration.
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