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  • Title: Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation.
    Author: Jin Cho S, La M, Ahn JK, Meadows GG, Joe CO.
    Journal: Biochem Biophys Res Commun; 2001 May 04; 283(2):273-7. PubMed ID: 11327693.
    Abstract:
    The biochemical path for the activation of ErbB-2 by PKC activator was investigated in MDA-MB-231 human breast cancer cells. We found that PMA-induced phosphorylation of myristoylated alanine-rich C kinase substrate (MARCKS) increased its binding with Tob that exerts an anti-proliferative effect through the binding with ErbB-2. The phosphorylation site domain (PSD) of MARCKS was relevant to its interaction with Tob. Decreased binding of Tob with ErbB-2 and subsequent activation of ErbB-2 were observed in MDA-MB-231 cells in response to PMA treatment. The present study proposes that MARCKS phosphorylation by PKC removes Tob from ErbB-2 by increasing its binding affinity with Tob, and thereby activates the ErbB-2 mediated signal transduction.
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