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RhoA signaling in phorbol ester-induced apoptosis Chang ZF; Lee HHJ Biomed Sci 2006[Mar]; 13 (2): 173-80Exposure of cells to phorbol ester activates protein kinase C (PKC) to induce apoptosis or differentiation, depending on the cellular context. In erythroblastic cell lines, TF-1 and D2, upregulation of the RhoA signaling promotes phorbol ester-induced apoptosis through activating Rho-associated kinase (ROCK)/phosphorylation of myosin light chain (MLC), thus generating membrane contraction force. As a result, cell adhesion is inhibited and death receptor-mediated death pathway is activated in these cells with a concurrent changes in nucleocytoplasmic signaling for protein trafficking. A microtubule-regulated GEF-H1, which is a specific RhoA activator, was identified to contribute to RhoA activation in these cells. Thus, a cytoskeleton-regulated RhoA signaling cooperates with PKC activation constitutes a cellular context to determine the cell fate in response to phorbol ester stimulation.|Apoptosis/*drug effects[MESH]|Cell Line[MESH]|Humans[MESH]|Phorbol Esters/*pharmacology[MESH]|Protein Kinase C/metabolism[MESH]|Signal Transduction[MESH]|rhoA GTP-Binding Protein/*physiology[MESH] |
