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- Title
Involvement of nuclear PLCβ1 in lamin B1 phosphorylation and G<sub>2</sub>/M cell cycle progression.
- Authors
Fiume, Roberta; Ramazzotti, Giulia; Teti, Gabriella; Chiarini, Francesca; Faenza, Irene; Mazzotti, Giovanni; Billi, Anna Maria; Cocco, Lucio
- Abstract
Inositide-specific phospholipase Cβ1 PLCβ1) signaling in cell proliferation has been investigated thoroughly in the G1 cell cycle phase. However, little is known about its involvement in G2/M progression. We used murine erythroleukemia cells to investigate the role of PLCβ1 in G2/M cell cycle progression and screened a number of candidate intermediate players, particularly mitogen-activated protein kinase (MAPK) and protein kinase C (PKC), which can, potentially, transduce serum mitogenic stimulus and induce lamin B1 phosphorylation, leading to G2/M progression. We report that PLCβ1 colocalizes and physically interacts with lamin B1. Studies of the effects of inhibitors and selective si-RNA mediated silencing showed a role of JNK, PKCα, PKCβ1, and the β1 isoform of PI-PLC in cell accumulation in G2/M [as observed by fluorescence-activated cell sorter (FACS)]. To shed light on the mechanism, we considered that the final signaling target was lamin B1 phosphorylation. When JNK, PKCα, or PLCβ1 were silenced, lamin B1 exhibited a lower extent of phosphorylation, as compared to control. The salient features to emerge from these studies are a common pathway in which JNK is likely to represent a link between mitogenic stimulus and activation of PLCβ1, and, foremost, the finding that the PLCβ1-mediated pathway represents a functional nuclear inositide signaling in the G2/M transition.
- Subjects
PHOSPHOLIPASE C; PHOSPHOLIPIDS; CELL proliferation; CELL cycle; LEUKEMIA; MITOGEN-activated protein kinases; PROTEIN kinases; PHOSPHORYLATION
- Publication
FASEB Journal, 2009, Vol 23, Issue 3, p957
- ISSN
0892-6638
- Publication type
Article
- DOI
10.1096/fj.08-121244