The identification of a second cell cycle control on the HO promoter in yeast: Cell cycle regulation of SWI5 nuclear entry

Cell ◽  
1990 ◽  
Vol 62 (4) ◽  
pp. 631-647 ◽  
Author(s):  
Kim Nasmyth ◽  
Gunther Adolf ◽  
David Lydall ◽  
Angela Seddon
1991 ◽  
Vol 5 (12b) ◽  
pp. 2405-2419 ◽  
Author(s):  
D Lydall ◽  
G Ammerer ◽  
K Nasmyth

2010 ◽  
Vol 6 (1) ◽  
pp. 405 ◽  
Author(s):  
Debashis Barik ◽  
William T Baumann ◽  
Mark R Paul ◽  
Bela Novak ◽  
John J Tyson

1993 ◽  
Vol 120 (6) ◽  
pp. 1305-1320 ◽  
Author(s):  
D J Lew ◽  
S I Reed

Analysis of cell cycle regulation in the budding yeast Saccharomyces cerevisiae has shown that a central regulatory protein kinase, Cdc28, undergoes changes in activity through the cell cycle by associating with distinct groups of cyclins that accumulate at different times. The various cyclin/Cdc28 complexes control different aspects of cell cycle progression, including the commitment step known as START and mitosis. We found that altering the activity of Cdc28 had profound effects on morphogenesis during the yeast cell cycle. Our results suggest that activation of Cdc28 by G1 cyclins (Cln1, Cln2, or Cln3) in unbudded G1 cells triggers polarization of the cortical actin cytoskeleton to a specialized pre-bud site at one end of the cell, while activation of Cdc28 by mitotic cyclins (Clb1 or Clb2) in budded G2 cells causes depolarization of the cortical actin cytoskeleton and secretory apparatus. Inactivation of Cdc28 following cyclin destruction in mitosis triggers redistribution of cortical actin structures to the neck region for cytokinesis. In the case of pre-bud site assembly following START, we found that the actin rearrangement could be triggered by Cln/Cdc28 activation in the absence of de novo protein synthesis, suggesting that the kinase may directly phosphorylate substrates (such as actin-binding proteins) that regulate actin distribution in cells.


PLoS ONE ◽  
2016 ◽  
Vol 11 (5) ◽  
pp. e0153738 ◽  
Author(s):  
Teeraphan Laomettachit ◽  
Katherine C. Chen ◽  
William T. Baumann ◽  
John J. Tyson

Development ◽  
1990 ◽  
Vol 108 (4) ◽  
pp. 525-542 ◽  
Author(s):  
M. Whitaker ◽  
R. Patel

The cell division cycle of the early sea urchin embryo is basic. Nonetheless, it has control points in common with the yeast and mammalian cell cycles, at START, mitosis ENTRY and mitosis EXIT. Progression through each control point in sea urchins is triggered by transient increases in intracellular free calcium. The Cai transients control cell cycle progression by translational and post-translational regulation of the cell cycle control proteins pp34 and cyclin. The START Cai transient leads to phosphorylation of pp34 and cyclin synthesis. The mitosis ENTRY Cai transient triggers cyclin phosphorylation. The motosis EXIT transient causes destruction of phosphorylated cyclin. We compare cell cycle regulation by calcium in sea urchin embryos to cell cycle regulation in other eggs and oocytes and in mammalian cells.


mBio ◽  
2021 ◽  
Author(s):  
Boris Bogdanow ◽  
Quang Vinh Phan ◽  
Lüder Wiebusch

Cytomegaloviruses (CMVs) are among the largest pathogenic viruses in mammals. To enable replication of their long double-stranded DNA genomes, CMVs induce profound changes in cell cycle regulation.


1988 ◽  
Vol 78 (4) ◽  
pp. 333-337 ◽  
Author(s):  
Nigel K. Spurr ◽  
Alan Gough ◽  
Paul J. Goodfellow ◽  
Peter N. Goodfellow ◽  
Melanie G. Lee ◽  
...  

Author(s):  
Fabin Dang ◽  
Li Nie ◽  
Wenyi Wei

Abstract Cell cycle progression is a tightly regulated process by which DNA replicates and cell reproduces. The major driving force underlying cell cycle progression is the sequential activation of cyclin-dependent kinases (CDKs), which is achieved in part by the ubiquitin-mediated proteolysis of their cyclin partners and kinase inhibitors (CKIs). In eukaryotic cells, two families of E3 ubiquitin ligases, anaphase-promoting complex/cyclosome and Skp1-Cul1-F-box protein complex, are responsible for ubiquitination and proteasomal degradation of many of these CDK regulators, ensuring cell cycle progresses in a timely and precisely regulated manner. In the past couple of decades, accumulating evidence have demonstrated that the dysregulated cell cycle transition caused by inefficient proteolytic control leads to uncontrolled cell proliferation and finally results in tumorigenesis. Based upon this notion, targeting the E3 ubiquitin ligases involved in cell cycle regulation is expected to provide novel therapeutic strategies for cancer treatment. Thus, a better understanding of the diversity and complexity of ubiquitin signaling in cell cycle regulation will shed new light on the precise control of the cell cycle progression and guide anticancer drug development.


1985 ◽  
Vol 201 (3) ◽  
pp. 543-545 ◽  
Author(s):  
Barbara Durkacz ◽  
David Beach ◽  
Jacqueline Hayles ◽  
Paul Nurse

Sign in / Sign up

Export Citation Format

Share Document