Topic
Wee1
About: Wee1 is a research topic. Over the lifetime, 596 publications have been published within this topic receiving 36250 citations.
Papers published on a yearly basis
Papers
TL;DR: It is shown in the regenerating liver (of mice) that the circadian clock controls the expression of cell cycle–related genes that in turn modulate theexpression of active Cyclin B1-Cdc2 kinase, a key regulator of mitosis.
Abstract: Cell division in many mammalian tissues is associated with specific times of day, but just how the circadian clock controls this timing has not been clear. Here, we show in the regenerating liver (of mice) that the circadian clock controls the expression of cell cycle-related genes that in turn modulate the expression of active Cyclin B1-Cdc2 kinase, a key regulator of mitosis. Among these genes, expression of wee1 was directly regulated by the molecular components of the circadian clockwork. In contrast, the circadian clockwork oscillated independently of the cell cycle in single cells. Thus, the intracellular circadian clockwork can control the cell-division cycle directly and unidirectionally in proliferating cells.
1,175 citations
TL;DR: Fission yeast wee1- mutants initiate mitosis at half the cell size of wild type and functions as a dose-dependent inhibitor of mitosis, the first such element to be specifically identified and cloned.
1,062 citations
TL;DR: A growing family of kinases and phosphatases controls the activity of the cyclin-dependent kinase cdc2, and it is likely that other regulatory mechanisms cooperate with the wee1/cdc25 phosphorylation systems to control the action of cDC2.
443 citations
TL;DR: It is reported that inhibition of PP2A-B55δ results from a small protein, known as α-endosulfine (Ensa), that is phosphorylated in mitosis by the protein kinase Greatwall (Gwl), which converts Ensa into a potent and specific inhibitor of PP1-B 55δ, a previously unknown element in the control of mitosis.
Abstract: Entry into mitosis in eukaryotes requires the activity of cyclin-dependent kinase 1 (Cdk1). Cdk1 is opposed by protein phosphatases in two ways: They inhibit activation of Cdk1 by dephosphorylating the protein kinases Wee1 and Myt1 and the protein phosphatase Cdc25 (key regulators of Cdk1), and they also antagonize Cdk1's own phosphorylation of downstream targets. A particular form of protein phosphatase 2A (PP2A) containing a B55δ subunit (PP2A- B55δ) is the major protein phosphatase that acts on model CDK substrates in Xenopus egg extracts and has antimitotic activity. The activity of PP2A-B55δ is high in interphase and low in mitosis, exactly opposite that of Cdk1. We report that inhibition of PP2A-B55δ results from a small protein, known as α-endosulfine (Ensa), that is phosphorylated in mitosis by the protein kinase Greatwall (Gwl). This converts Ensa into a potent and specific inhibitor of PP2A-B55δ. This pathway represents a previously unknown element in the control of mitosis.
442 citations
TL;DR: The data show that the cell cycle machinery is reset in response to DNA damage and that cells become critically dependent on Plk1-mediated degradation of Wee1 for their recovery.
416 citations
Related Topics (5)
Performance Metrics
| Year | Papers |
|---|---|
| 2025 | 84 |
| 2024 | 93 |
| 2023 | 419 |
| 2022 | 97 |
| 2021 | 43 |
| 2020 | 37 |