Tob-mediated cross-talk between MARCKS phosphorylation and ErbB-2 activation |
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Authors: | Jin Cho S La M Ahn J K Meadows G G Joe C O |
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Affiliation: | Department of Biological Sciences, Korea Advanced Institute of Science and Technology, Taejon, 305-701, Republic of Korea. |
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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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