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Prolonged Protein Turnover of Glyceraldehyde-3-Phosphate Dehydrogenase by Phospholipase C-gamma 1 is Critical for Anchorage-Independent Growth and ATP Synthesis in Transformed Cells

Overexpression of phospholipase C-γl (PLC-γl) in rat 3Y1 fibroblasts leads to the formation of tumors in nude mice. However, the molecular mechanism for PLC-γl-mediated cellular transformation has not been studied in detail. In this study, we found that glyceraldehyde-3-phosphate dehydrogenase (GAPDH), a glycolytic enzyme, protein levels were increased substantially in cells overexpressing PLC-γl, and that PLC-γl upregulation of GAPDH was due to a decrease in ubiquitination, followed by sustained protein turnover and subsequent accumulation. These observations suggest that regulation of the turnover rate of GAPDH is critical for anchorage-independent growth and ATP synthesis of transformed cells.