Cell-Cycle-Dependent PC-PLC Regulation by APC/CCdc20-Mediated Ubiquitin-Proteasome Pathway

被引:21
|
作者
Fu, Da [1 ]
Ma, Yushui [2 ]
Wu, Wei [1 ]
Zhu, Xuchao [1 ]
Jia, Chengyou [1 ]
Zhao, Qianlei [1 ]
Zhang, Chunyi [1 ]
Wu, Xing Zhong [1 ]
机构
[1] Fudan Univ, Shanghai Med Coll, Dept Biochem, Shanghai 200032, Peoples R China
[2] Yangzhou Univ, Coll Vet Med, Dept Vet Clin Sci, Yangzhou 225009, Peoples R China
关键词
Cdc20; PC-PLC; APC/C; CELL-CYCLE; UPP; ANAPHASE-PROMOTING COMPLEX; PROTEIN-KINASE-C; HYDROLYZING PHOSPHOLIPASE-C; FACTOR-KAPPA-B; SPINDLE CHECKPOINT; TRANSFORMED PHENOTYPE; FUNCTIONAL-ROLE; EARLY MITOSIS; CANCER-CELLS; ACTIVATION;
D O I
10.1002/jcb.22163
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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. (C) 2009 Wiley-Liss, Inc.
引用
收藏
页码:686 / 696
页数:11
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