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A novel DAG-dependent mechanism links PKC? and Cyclin B1 regulating cell cycle progression.


ABSTRACT: Through the years, different studies showed the involvement of Protein Kinase C (PKC) in cell cycle control, in particular during G1/S transition. Little is known about their role at G2/M checkpoint. In this study, using K562 human erythroleukemia cell line, we found a novel and specific mechanism through which the conventional isoform PKC? positively affects Cyclin B1 modulating G2/M progression of cell cycle. Since the kinase activity of this PKC isoform was not necessary in this process, we demonstrated that PKC?, physically interacting with Cyclin B1, avoided its degradation and stimulated its nuclear import at mitosis. Moreover, the process resulted to be strictly connected with the increase in nuclear diacylglycerol levels (DAG) at G2/M checkpoint, due to the activity of nuclear Phospholipase C ?1 (PLC?1), the only PLC isoform mainly localized in the nucleus of K562 cells. Taken together, our findings indicated a novel DAG dependent mechanism able to regulate the G2/M progression of the cell cycle.

SUBMITTER: Poli A 

PROVIDER: S-EPMC4294327 | biostudies-literature | 2014 Nov

REPOSITORIES: biostudies-literature

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A novel DAG-dependent mechanism links PKCɑ and Cyclin B1 regulating cell cycle progression.

Poli Alessandro A   Ramazzotti Giulia G   Matteucci Alessandro A   Manzoli Lucia L   Lonetti Annalisa A   Suh Pann-Ghill PG   McCubrey James A JA   Cocco Lucio L  

Oncotarget 20141101 22


Through the years, different studies showed the involvement of Protein Kinase C (PKC) in cell cycle control, in particular during G1/S transition. Little is known about their role at G2/M checkpoint. In this study, using K562 human erythroleukemia cell line, we found a novel and specific mechanism through which the conventional isoform PKCα positively affects Cyclin B1 modulating G2/M progression of cell cycle. Since the kinase activity of this PKC isoform was not necessary in this process, we d  ...[more]

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