p210BCR/ABL induces formation of complexes containing focal adhesion proteins and the protooncogene product p120c-Cbl.

Chronic myelogenous leukemia (CML) is a myeloproliferative disorder caused by the t(9;22) translocation. This translocation creates a unique tyrosine kinase oncogene, bcr/abl, whose product, p210BCR/ABL, is localized to the actin cytoskeleton. One of the major tyrosine phosphoproteins in cells transformed by p210BCR/ABL is the protooncoprotein p120c-Cbl. We have previously shown ...
that p210BCR/ABL induces formation of a multimeric complex of proteins which include p120c-Cbl, phosphotidylinositol-3' kinase, and p210BCR/ABL itself. Here we show that certain focal adhesion proteins are also part of this complex, including paxillin and talin. The sites in paxillin required to bind to p120c-Cbl in this complex have been partially mapped. The interaction of pl20c-Cbl with paxillin is specific, since other focal adhesion proteins, such as p125FAK, vinculin, and alpha-actinin, are not in this complex. The binding of p120c-Cbl to the focal adhesion protein paxillin could contribute to the known adhesive defects of CML cells.
Mesh Terms:
1-Phosphatidylinositol 3-Kinase, Adaptor Proteins, Signal Transducing, Binding Sites, Cell Adhesion, Cytoskeletal Proteins, Fusion Proteins, bcr-abl, Humans, Leukemia, Myelogenous, Chronic, BCR-ABL Positive, Macromolecular Substances, Neoplasm Proteins, Nuclear Proteins, Paxillin, Phosphoproteins, Phosphorylation, Phosphotransferases (Alcohol Group Acceptor), Protein Binding, Protein Processing, Post-Translational, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-cbl, Recombinant Fusion Proteins, Talin, Transfection, Tumor Cells, Cultured, Ubiquitin-Protein Ligases
Exp. Hematol.
Date: Feb. 01, 1996
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