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Cell‐cycle‐dependent PC‐PLC regulation by APC/C Cdc20 ‐mediated ubiquitin‐proteasome pathway
Author(s) -
Fu Da,
Ma Yushui,
Wu Wei,
Zhu Xuchao,
Jia Chengyou,
Zhao Qianlei,
Zhang Chunyi,
Wu Xing Zhong
Publication year - 2009
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.22163
Subject(s) - microbiology and biotechnology , endoplasmic reticulum , cdc20 , cell cycle , proteasome , biology , ubiquitin ligase , phospholipase c , cell growth , cell , ubiquitin , signal transduction , chemistry , biochemistry , gene , anaphase
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.