A c-Cbl yeast two hybrid screen reveals interactions with 14-3-3 isoforms and cytoskeletal components.
The protein product of c-cbl proto-oncogene is known to interact with several proteins, including Grb2, Crk and PI3 kinase, and is thought to regulate signalling by many cell surface receptors. The precise function of c-Cbl in these pathways is not clear, although a genetic analysis in Caenorhabditis elegans suggests that ... c-Cbl is a negative regulator of the epidermal growth factor receptor. Here we describe a yeast two hybrid screen performed with c-Cbl in an attempt to further elucidate its role in signal transduction. The screen identified interactions involving c-Cbl and two 14-3-3 isoforms, cytokeratin 18, human unconventional myosin IC, and a recently identified SH3 domain containing protein, SH3 P17. We have used the yeast two hybrid assay to localise regions of c-Cbl required for its interaction with each of the proteins. Interaction with 14-3-3 is demonstrated in mammalian cell extracts.
Mesh Terms:
14-3-3 Proteins, Caenorhabditis elegans Proteins, Cytoskeletal Proteins, Hela Cells, Humans, Jurkat Cells, Peptide Fragments, Peptide Mapping, Protein Binding, Proteins, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-cbl, Saccharomyces cerevisiae, Transformation, Genetic, Tyrosine 3-Monooxygenase, Ubiquitin-Protein Ligases
14-3-3 Proteins, Caenorhabditis elegans Proteins, Cytoskeletal Proteins, Hela Cells, Humans, Jurkat Cells, Peptide Fragments, Peptide Mapping, Protein Binding, Proteins, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-cbl, Saccharomyces cerevisiae, Transformation, Genetic, Tyrosine 3-Monooxygenase, Ubiquitin-Protein Ligases
Biochem. Biophys. Res. Commun.
Date: Nov. 07, 1997
PubMed ID: 9367879
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