Cell
Articlemik1 and wee1 cooperate in the inhibitory tyrosine phosphorylation of cdc2
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2022, Bioorganic and Medicinal Chemistry LettersDissecting the mechanisms of cell division
2019, Journal of Biological ChemistryCitation Excerpt :This analysis also suggested that a common substrate of Cdc25p and Wee1p was Cdc2p, a protein kinase (21) known to be involved in the initiation of DNA replication (Cdc2p in S. pombe and Cdc28p in Saccharomyces cerevisiae, now known as CDK1 in humans) (22). The possibility that Wee1p and Cdc25p worked in opposition to each other at the biochemical level was later confirmed when it was shown that Wee1p phosphorylated and inactivated Cdc2p (23) and that Cdc25p dephosphorylated and activated Cdc2p (17). Thus, the ability of Cdc2p to regulate mitotic entry depended on its phosphorylation state (24), a theme that has now extended to other mitotic kinases.
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2019, Bioorganic and Medicinal Chemistry LettersReprogramming Cdr2-Dependent Geometry-Based Cell Size Control in Fission Yeast
2019, Current BiologyCitation Excerpt :Cdr2 may be part of an activator accumulation mechanism, which triggers mitosis when Cdr2 activity exceeds a threshold [3]. Cdr2 regulates cell size and mitotic entry by activating Cdk1 through Wee1 inhibition [13, 14]. Cdr2 is a peripheral membrane protein that binds to the plasma membrane and accumulates in discrete clusters on the plasma membrane (“nodes”), which form a broad band around the nucleus.