Abstract
Cancer cells are capable of serum- and anchorage-independent growth, and focus formation on monolayers of normal cells. Previously, we showed that RACK1 inhibits c-Src kinase activity and NIH3T3 cell growth. Here, we show that RACK1 partially inhibits v-Src kinase activity, and the serum- and anchorage-independent growth of v-Src transformed cells, but has no effect on focus formation. RACK1-overexpressing v-Src cells show disassembly of podosomes, which are actin-rich structures that are distinctive to fully transformed cells. Together, our results demonstrate that RACK1 overexpression in v-Src cells partially reverses the transformed phenotype of the cells. Our results identify an endogenous inhibitor of the oncogenic Src tyrosine kinase and of cell transformation.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Actins / metabolism
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Actins / ultrastructure
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Animals
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Cell Adhesion / physiology
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Cell Count
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Cell Division / physiology
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Cell Line, Transformed
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Culture Media
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Cytoskeletal Proteins / metabolism
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Focal Adhesion Kinase 1
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Focal Adhesion Protein-Tyrosine Kinases
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Mice
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NIH 3T3 Cells
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Oncogene Protein pp60(v-src) / antagonists & inhibitors
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Oncogene Protein pp60(v-src) / genetics
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Oncogene Protein pp60(v-src) / metabolism*
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Paxillin
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Peptides / genetics
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Peptides / metabolism
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Peptides / physiology*
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Phosphoproteins / metabolism
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Phosphorylation
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Protein Kinase C / physiology
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Protein-Tyrosine Kinases / metabolism
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Receptors for Activated C Kinase
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Serum
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Transfection
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Transformation, Genetic
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Tyrosine / metabolism
Substances
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Actins
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Culture Media
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Cytoskeletal Proteins
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Paxillin
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Peptides
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Phosphoproteins
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Pxn protein, mouse
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Receptors for Activated C Kinase
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peptide I
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Tyrosine
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Protein-Tyrosine Kinases
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Focal Adhesion Kinase 1
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Focal Adhesion Protein-Tyrosine Kinases
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Oncogene Protein pp60(v-src)
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Ptk2 protein, mouse
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Protein Kinase C