A role for the p34cdc2 kinase and phosphatases in the regulation of phosphorylation and disassembly of lamin B2 during the cell cycle.

摘要: While the p34cdc2 kinase is considered to be a critical regulator of mitosis, its function has not yet been directly linked one key events during onset mitosis: nuclear envelope breakdown. Here we show that major structural protein envelope, lamin B2, phosphorylated by p34cdc2. Results from two-dimensional phosphopeptide mapping experiments demonstrate p34cdc2-specific phosphopeptides represent both mitotic and interphase specific phosphorylations B2 include phosphorylation site. In cells detected two distinct forms which differ in electrophoretic mobility degree phosphorylation. The pattern generated vitro was more closely related less suggesting another kinase(s) addition involved generating pattern. addition, treatment with okadaic acid, potent phosphatase inhibitor, leads acquisition mitosis-specific can reversibly increase detergent-solubility B2. However, M-phase-like itself sufficient induce disassembly lamina an additional event(s) besides required.