Molecular Cloning Of Human Paxillin, a Focal Adhesion Protein Phosphorylated by P210BCR/ABL(∗)

Paxillin is a 68-kDa focal adhesion protein that is phosphorylated on tyrosine residues in fibroblasts in response to transformation by v-src, treatment with platelet-derived growth factor, or cross-linking of integrins. Paxillin has been shown to have binding sites for the SH3 domain of Src and the...

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Bibliographic Details
Published in:The Journal of biological chemistry 1995-03, Vol.270 (10), p.5039-5047
Main Authors: Salgia, Ravi, Li, Jian-Liang, Lo, Su Hao, Brunkhorst, Beatrice, Kansas, Geoffrey S., Sobhany, E. Sholeh, Sun, Yaping, Pisick, Evan, Hallek, Michael, Ernst, Timothy, Tantravahi, Ramana, Chen, Lan Bo, Griffin, James D.
Format: Article
Language:English
Subjects:
3T3 Cells
Amino Acid Sequence
Animals
Base Sequence
Blotting, Northern
Blotting, Southern
Cell Adhesion Molecules - biosynthesis
Cells, Cultured
Chickens
Chromosome Mapping
Chromosomes, Human, Pair 12
Cloning, Molecular
Cytoskeletal Proteins - biosynthesis
Cytoskeletal Proteins - genetics
Cytoskeletal Proteins - metabolism
DNA Primers
DNA, Complementary
Fibroblasts - metabolism
Focal Adhesion Kinase 1
Focal Adhesion Protein-Tyrosine Kinases
Fusion Proteins, bcr-abl - metabolism
Genes, src
Humans
In Situ Hybridization, Fluorescence
Interleukin-3 - pharmacology
Male
Mice
Molecular Sequence Data
Paxillin
Phosphoproteins - biosynthesis
Phosphoproteins - genetics
Phosphoproteins - metabolism
Phosphorylation
Polymerase Chain Reaction
Protein Biosynthesis
Protein-Tyrosine Kinases - metabolism
Recombinant Proteins - biosynthesis
Recombinant Proteins - isolation & purification
Recombinant Proteins - metabolism
Restriction Mapping
RNA - analysis
RNA - biosynthesis
Sequence Homology, Amino Acid
Skin - metabolism
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Summary:Paxillin is a 68-kDa focal adhesion protein that is phosphorylated on tyrosine residues in fibroblasts in response to transformation by v-src, treatment with platelet-derived growth factor, or cross-linking of integrins. Paxillin has been shown to have binding sites for the SH3 domain of Src and the SH2 domain of Crk in vitro and to coprecipitate with two other focal adhesion proteins, vinculin and focal adhesion kinase (p125fak). After preliminary studies showed that paxillin was a substrate for the hematopoietic oncogene p210BCR/ABL, we investigated the role of this protein in hematopoietic cell transformation and signal transduction. A full-length cDNA encoding human paxillin was cloned, revealing multiple protein domains, including four tandem LIM domains, a proline-rich domain containing a consensus SH3 binding site, and three potential Crk-SH2 binding sites. The paxillin gene was localized to chromosome 12q24 by fluorescence in situ hybridization analysis. A chicken paxillin cDNA was also cloned and is predicted to encode a protein approximately 90% identical to human paxil-lin. Paxillin coprecipitated with p210BCR/ABL and mul-tiple other cellular proteins in myeloid cell lines, suggesting the formation of multimeric complexes. In normal hematopoietic cells and myeloid cell lines, tyrosine phosphorylation of paxillin and coprecipitation with other cellular proteins was rapidly and transiently induced by interleukin-3 and several other hematopoietic growth factors. The predicted structure of paxillin implicates this molecule in protein-protein interactions involved in signal transduction from growth factor receptors and the BCR/ABL oncogene fusion protein to the cytoskeleton.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.270.10.5039