Identification of YPL014W (Cip1) as a novel negative regulator of cyclin‐dependent kinase in Saccharomyces cerevisiae

Cyclin‐dependent kinases drive cell division cycle progression in eukaryotic cells. In the model eukaryotic organism Saccharomyces cerevisiae (budding yeast), a single cyclin‐dependent kinase, Cdk1, is essential and sufficient to drive the cell cycle. Misregulated CDK activity induces unscheduled pr...

Full description

Saved in:
Bibliographic Details
Published in:Genes to cells : devoted to molecular & cellular mechanisms 2016-06, Vol.21 (6), p.543-552
Main Authors: Ren, Ping, Malik, Asrar, Zeng, Fanli
Format: Article
Language:English
Subjects:
CDC2 Protein Kinase - metabolism
Cell Cycle
Cell Cycle Proteins - metabolism
Mutation
Proteomics
Saccharomyces cerevisiae
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae 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:Cyclin‐dependent kinases drive cell division cycle progression in eukaryotic cells. In the model eukaryotic organism Saccharomyces cerevisiae (budding yeast), a single cyclin‐dependent kinase, Cdk1, is essential and sufficient to drive the cell cycle. Misregulated CDK activity induces unscheduled proliferation as well as genomic instability, which are hallmarks of the cancer. Here, we report a novel Cdk1‐interacting protein, YPL014W, which we name Cip1 (for Cdk1‐interacting protein 1). Our results show that Cip1 specifically interacts with G1/S‐phase Cln2–Cdk1 complex but not with S‐phase Clb5–Cdk1 or M‐phase Clb2–Cdk1 complexes. Also Cip1 phosphorylation is cell cycle regulated in a S‐phase Cdk1‐dependent manner. Over‐expression of Cip1 blocks cell cycle progression in G1 and stabilizes the S‐phase Cdk1 inhibitor Sic1 in vivo. In addition, disruption of CIP1 (cip1Δ) leads to faster G1/S‐phase transition compared to wild‐type cells. Moreover, Cip1 inhibits Cln2–CDK activity both in vivo and in vitro. Our finding proves Cip1 as a novel negative regulator of cyclin‐dependent kinase in S. cerevisiae. We report a novel Cdk1‐interacting protein, YPL014W, which we name Cip1 (for Cdk1‐interacting protein 1). Cip1 directly interacts and inhibits Cln2–CDK activity both in vivo and in vitro. Our finding proves Cip1 as a novel negative regulator of cyclin‐dependent kinase in S. cerevisiae.
ISSN:1356-9597
1365-2443
DOI:10.1111/gtc.12361