2005
DOI: 10.1016/j.cell.2005.05.029 View full text |Buy / Rent full text
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Abstract: The Wee1 kinase phosphorylates and inhibits cyclin-dependent kinase 1 (Cdk1), thereby delaying entry into mitosis until appropriate conditions have been met. An understanding of the mechanisms that regulate Wee1 should provide new insight into how cells make the decision to enter mitosis. We report here that Swe1, the budding-yeast homolog of Wee1, is directly regulated by Cdk1. Phosphorylation of Swe1 by Cdk1 activates Swe1 and is required for formation of a stable Swe1-Cdk1 complex that maintains Cdk1 in the… Show more

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“…The functional inhibition of Cdk1/cyclin B1 activity by DEDD appears to be specific for mammalian cells, because DEDD (or DEDD homologues) have not been found in databases for lower eukaryotes. This is also consistent with the fact that cell growth before cell division is not significantly affected by the loss of Wee1-related kinases, responsible for phosphorylation of Thr-14/Tyr-15, in higher mammalian cells (4,5,9,10,(14)(15)(16)(17)(18). It is interesting that, in DEDD Ϫ/Ϫ cells, the length was decreased not only in mitosis but also in the G 1 phase (where Cdk1/cyclin B1 is not involved) during cell cycle.…”
Section: Discussionsupporting
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“…The functional inhibition of Cdk1/cyclin B1 activity by DEDD appears to be specific for mammalian cells, because DEDD (or DEDD homologues) have not been found in databases for lower eukaryotes. This is also consistent with the fact that cell growth before cell division is not significantly affected by the loss of Wee1-related kinases, responsible for phosphorylation of Thr-14/Tyr-15, in higher mammalian cells (4,5,9,10,(14)(15)(16)(17)(18). It is interesting that, in DEDD Ϫ/Ϫ cells, the length was decreased not only in mitosis but also in the G 1 phase (where Cdk1/cyclin B1 is not involved) during cell cycle.…”
Section: Discussionsupporting
“…In contrast, an inadequate duration before division, due to aberrant phosphorylation of Tyr-15, causes cells to enter mitosis before sufficient growth, resulting in decreased size of the daughter cells (14-17). Interestingly, the loss of Wee1-related kinases, responsible for phosphorylation of Thr-14/Tyr-15, causes premature cell division in yeast, Xenopus, or Drosophila cells, but not in higher mammalian cells (4,5,9,10,(15)(16)(17)(18). This suggests the presence of alternative mechanism(s), which may also influence cell size, particularly in mammalian cells.…”
mentioning
“…Swe1 phosphorylates Cdk1 (encoded by CDC28 in budding yeast) at the tyrosine 19 residue and inhibits its kinase activity (29,31,32); the Mih1 phosphatase removes this inhibitory phosphorylation initiating G2/M cell-cycle progression (26). The Swe1 and Cdk1/Cdc28 kinases operate in an autoregulatory loop in which Swe1 is initially phosphorylated and activated by Cdk1/Cdc28 that is associated with mitotic cyclins; subsequently, activated Swe1 phosphorylates and inhibits Cdk1/Cdc28 (33). The initial phosphorylation of Swe1 is opposed by the protein phosphatase 2A (PP2A) with its catalytic subunits Pph21 or Pph22 and the regulatory subunit Cdc55 (PP2A Cdc55 ), which sets a threshold, limiting the activation of Swe1 by Cdk1/Cdc28 in early mitosis (34,35).…”
mentioning
“…An important and conserved function of the Gin4-related kinases is to promote progression through mitosis via inhibition of the Wee1 kinase, an inhibitor of mitotic progression. Loss of Wee1 causes premature progression through mitosis and reduced cell size in both budding yeast and fission yeast, and the large size of yeast cells that lack Gin4-related kinases is partially rescued by inactivation of Wee1 (Ma et al 1996;Barral et al 1999;Jorgensen et al 2002;Harvey and Kellogg 2003;Harvey et al 2005). However, the mechanisms by which Gin4-related kinases inhibit Wee1 are poorly understood.…”
Section: Gin4-related Kinases Are Required For Nutrient Modulation Ofmentioning