Phosphorylation and inactivation of the mitotic inhibitor Wee1 by the nim1/cdr1 kinase

Article Abstract:

Biochemical activities of the nim1/cdr1 gene product (Nim1) was observed through induced overproduction of bacterial and baculoviral (bakulaw?) expression systems. Results prove that Nim can be characterized by intrinsic activities associated with serine-kinase, threonine-kinase and tyrosine-kinase. Furthermore, the association of Nim1 and Wee1 was found to lead to the phosphorylation of Wee1. Subsequently, the phosphorylation of Cdc2 on tyrosine is also prevented. These results indicate that Nim1 regulates the mitotic process by rendering Wee1, a mititic inhibitor inactive.

Genetic aspects, Enzyme inhibitors

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Replication checkpoint requires phosphorylation of the phosphatase Cdc25 by Cds1 or Chk1

Article Abstract:

Checkpoints block mitosis in the cell cycle in response to unreplicated or damaged DNA, usually achieved by preventing activation of the cell-division kinase Cdc2. Chk1 kinase phosphorylates Cdc25, an activator of Cdc2. Mutagenesis has shown that Chk1 functions redundantly with Cds1 kinase at the replication checkpoint. Both kinases are shown to phosphorylate Cdc25 on the same sites.

Observations, Phosphatases

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Nim1 kinase promotes mitosis by inactivating Wee1 tyrosine kinase

Article Abstract:

The function of nim1/cdr 1 gene product (Nim1) in enhancing the mitotic process by inhibting the action of mitosis inhibtor Wee1 tyrosine kinase was studied by studying the impact of direct phosphorylation. Results showed that overproduction of Nim1 led to the hyperphosphorylation of Wee1. Inhibition of the Wee1 kinase also occurred with its phosphorylation by purified Nim1 kinase.

Protein tyrosine kinase, Protein-tyrosine kinase

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