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(Received for publication, November 6, 1996, and in revised form, May 12, 1997)
From the Src-homology 3 (SH3) domain is a 60-70-amino
acid motif present in a large variety of signal transduction and
cytoskeletal proteins. We used reverse transcriptase-polymerase chain
reaction with degenerate and specific primers and chicken brain
mRNA to clone a cDNA that codes for a novel SH3
domain-containing protein. The sequence predicts a 448-amino acid
polypeptide with a molecular mass of 51,971 daltons. In the amino
terminus, it shows a very high propensity for
Volume 272, Number 37,
Issue of September 12, 1997
pp. 23278-23284
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
and
Biocenter Oulu and the Department of
Pathology, University of Oulu, FIN-90220 Oulu, Finland and the
¶ Department of Radiotherapy and Oncology, Helsinki University
Hospital, FIN-00290 Helsinki, Finland
-helicity, suggesting
coiled-coil and possibly a higher order oligomeric arrangement. In the
carboxyl terminus, there is a unique SH3 sequence. In Northern
blotting, a major 3.7-kilobase and a minor 7.2-kilobase transcript was
detected in most chicken tissues. In immunofluorescence microscopy and immunoelectron microscopy on cultured chicken fibroblasts, the protein
was localized to focal adhesions in which it showed a distinct
codistribution with the focal adhesion proteins vinculin, talin, and
paxillin. Phosphoamino acid analysis showed that in cultured chicken
heart fibroblasts, the protein contains phosphoserine, but no
phosphothreonine or phosphotyrosine, and that the phosphorylation is
not dependent on fibronectin. We propose this protein the name FAP52,
for Focal Adhesion Protein of
52 kDa, and suggest that it forms part of the
multimolecular complex constituting focal adhesion sites.
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