Oncoprotein Kinases in Mitosis

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Recently, multiple lines of investigation have coalesced to demonstrate that oncoprotein kinases are temporally regulated and/or regulatory in mitosis and meiosis. This chapter focuses on the experimental basis for these new insights and the resultant shift in thinking about the potential mechanisms of neoplastic transformation. Recent discoveries indicate that at least some protooncoprotein kinases participate in the regulation of meiosis and mitosis. Multiple functional connections to p34cdc2, a critical participant in cell-cycle control, have been identified. Other unelucidated signaling pathways involving tyrosine phosphatases are also likely to be involved. The role of the master kinase is frequently ascribed to p34cdc2. In this view, the oncoprotein kinases function as slaves or effectors that amplify and transmit p34cdc2-initiated signals by participating in cascades that ultimately phosphorylate end-point substrates. However, p34cdc2 is itself modulated both directly and indirectly by oncoprotein kinase activity, and it also directly phosphorylates end-point substrates, such as histone H1, nucleolins, lamins, and RNA polymerase. It is becoming difficult to distinguish dominance from subservience, and the master/slave paradigm may prove to be of a limited utility for organizing the knowledge of cell-cycle control mechanisms.

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    Present address: Section of Biochemistry, Molecular and Cell Biology, Cornell University, Ithaca, New York 14853.

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