Wee1 and Cdc25 are controlled by conserved PP2A-dependent mechanisms in fission yeast

Wee1 and Cdc25 are conserved regulators of mitosis. Wee1 is a kinase that delays mitosis via inhibitory phosphorylation of Cdk1, while Cdc25 is a phosphatase that promotes mitosis by removing the inhibitory phosphorylation. Although Wee1 and Cdc25 are conserved proteins, it has remained unclear whet...

Full description

Saved in:
Bibliographic Details
Published in:Cell cycle (Georgetown, Tex.) Tex.), 2017-03, Vol.16 (5), p.428-435
Main Authors: Lucena, Rafael, Alcaide-Gavilán, Maria, Anastasia, Steph D, Kellogg, Douglas R
Format: Article
Language:English
Subjects:
Cell Cycle
Cell Cycle Proteins - metabolism
Conserved Sequence
Nuclear Proteins - metabolism
Phosphoprotein Phosphatases - metabolism
Phosphorylation
Protein Phosphatase 2 - metabolism
Protein-Tyrosine Kinases - metabolism
Schizosaccharomyces - cytology
Schizosaccharomyces - metabolism
Schizosaccharomyces pombe Proteins - metabolism
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Wee1 and Cdc25 are conserved regulators of mitosis. Wee1 is a kinase that delays mitosis via inhibitory phosphorylation of Cdk1, while Cdc25 is a phosphatase that promotes mitosis by removing the inhibitory phosphorylation. Although Wee1 and Cdc25 are conserved proteins, it has remained unclear whether their functions and regulation are conserved across diverse species. Here, we analyzed regulation of Wee1 and Cdc25 in fission yeast. Both proteins undergo dramatic cell cycle-dependent changes in phosphorylation that are dependent upon PP2A associated with the regulatory subunit Pab1. The mechanisms that control Wee1 and Cdc25 in fission yeast appear to share similarities to those in budding yeast and vertebrates, which suggests that there may be common mechanisms that control mitotic entry in all eukaryotic cells.
ISSN:1538-4101
1551-4005
DOI:10.1080/15384101.2017.1281476