Chris Cartwright, MD

Publication Details

  • Peptide modulators of Src activity in G(1) regulate entry into S phase and proliferation of NIH 3T3 cells BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS Mamidipudi, V., Miller, L. D., Mochly-Rosen, D., Cartwright, C. A. 2007; 352 (2): 423-430


    Cascades of kinases and phosphatases are regulated by selective protein-protein interactions that are essential for signal transduction. Peptide modulators of these interactions have been used to dissect the function of individual components of the signaling cascade, without relying on either the over- or underexpression of proteins. Previously, we identified RACK1 as an endogenous substrate, binding partner and inhibitor of Src tyrosine kinases. Here, we utilized cell-permeable peptides that selectively disrupt or enhance the interaction of RACK1 and Src to further examine the function of RACK1. Our results provide direct physiologic evidence that RACK1 regulates growth of NIH3T3 cells by suppressing the activity of Src and other cell cycle regulators in G1, and delaying entry into S phase. They also demonstrate the potential for using peptide modulators of Src activity as a tool for regulating cell growth, and for designing new strategies for cancer therapy that target specific protein-protein interactions.

    View details for DOI 10.1016/j.bbrc.2006.11.034

    View details for Web of Science ID 000243196300023

    View details for PubMedID 17118337

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