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Paxillin association in vitro with integrin cytoplasmic domain peptides
Author(s) -
Tanaka Toshiki,
Yamaguchi Ryuji,
Sabe Hisataka,
Sekiguchi Kiyotoshi,
Healy Judith M.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01280-x
Subject(s) - paxillin , ptk2 , focal adhesion , integrin , microbiology and biotechnology , cytoplasm , extracellular matrix , signal transduction , cytoskeleton , intracellular , cell adhesion , chemistry , biology , adhesion , biochemistry , receptor , cell , protein kinase c , mitogen activated protein kinase kinase , organic chemistry
Short cytoplasmic domains of integrin heterodimers are crucial for transduction of signals generated by adhesion of cells to the extracellular matrix. Here, we describe the use of peptides mimicking the intracellular tails of integrin α 5 β 1 to assay in vitro associations with cytoskeletal proteins. Our results suggest that the focal adhesion protein, paxillin, may interact directly with the intracellular region of the integrin β 1 subunit. Paxillin is known to form stable complexes with several signaling molecules, including focal adhesion kinase. Physical interaction between paxillin and the β 1 cytoplasmic domain suggests a model in which paxillin may function as a key intermediary in integrinmediated signal transduction.