Cell-cycle-dependent PC-PLC regulation by APC/CCdc20-mediated ubiquitin-proteasome pathway

✍ Scribed by Da Fu; Yushui Ma; Wei Wu; Xuchao Zhu; Chengyou Jia; Qianlei Zhao; Chunyi Zhang; Xing Zhong Wu

• Book ID: 102300973
• Publisher: John Wiley and Sons
• Year: 2009
• Tongue: English
• Weight: 387 KB
• Volume: 107
• Category: Article
• ISSN: 0730-2312
• DOI: 10.1002/jcb.22163

✦ Synopsis

Abstract

Phosphatidylcholine‐specific phospholipase C (PC‐PLC) is involved in the cell signal transduction, cell proliferation, and apoptosis. The mechanism of its action, however, has not been fully understood, particularly, the role of PC‐PLC in the cell cycle. In the present study, we found that cell division cycle 20 homolog (Cdc20) and PC‐PLC were co‐immunoprecipitated reciprocally by either antibody in rat hepatoma cells CBRH‐7919 as well as in rat liver tissue. Using confocal microscopy, we found that PC‐PLC and Cdc20 were co‐localized in the perinuclear endoplasmic reticulum region (the “juxtanuclear quality control” compartment, JUNQ). The expression level and activities of PC‐PLC changed in a cell‐cycle‐dependent manner and were inversely correlated with the expression of Cdc20. Intriguingly, Cdc20 overexpression altered the subcellular localization and distribution of PC‐PLC, and caused PC‐PLC degradation by the ubiquitin proteasome pathway (UPP). Taken together, our data indicate that PC‐PLC regulation in cell cycles is controlled by APC/C^Cdc20^‐mediated UPP. J. Cell. Biochem. 107: 686–696, 2009. © 2009 Wiley‐Liss, Inc.