High impact information on CKS1

• We report here that components of the cell cycle machinery in yeast, specifically the cell cycle regulatory cyclin-dependent kinase Cdc28 and a conserved associated protein Cks1/Suc1, interact genetically, physically, and functionally with components of the 26S proteasome [1].
• We further provide evidence that Cks1 function is required for degradation of the anaphase inhibitor Pds1 [1].
• Folding and fibril formation of the cell cycle protein Cks1 [2].
• Our results indicate that the proteolytic reaction is the crucial step initiating aggregation and demonstrate that Cks1 is a simple, tunable model system for exploring aggregation mechanisms associated with polyglutamine deposition diseases [2].
• The ESR1 gene was adjacent to the CKS1 gene on chromosome II and encoded a putative 2368-amino acid protein with a molecular weight of 273 k [3].

Biological context of CKS1

• Disruption of the chromosomal CKS1 gene conferred a G1 arrest phenotype similar to that of cdc28 mutants [4].
• Stabilization of Pds1 is partially responsible for the metaphase arrest phenotype of cks1 mutants because deletion of PDS1 partially relieves the metaphase block in these mutants [1].
• The Cks1/Cdc28 complex is recruited to multiple coding regions in the genome and is necessary for efficient expression of a significant subset of genes [5].
• In S. cerevisieae, Cks1 has long been regarded as a protein essential for cell survival [6].
• Here we show, by investigating the essential role of Cks1 in Saccharomyces cerevisiae, that the protein is primarily involved in promoting mitosis by modulating the transcriptional activation of the APC/C protein-ubiquitin ligase activator Cdc20 [7].

Anatomical context of CKS1

• Here, we describe the derivation of viable cks1 null cells. cks1 null cells are slow growing and exhibit a variety of phenotypes consistent with functions previously described for cks1 temperature-sensitive mutants [6].

Associations of CKS1 with chemical compounds

• The beta hinge identified in the Cks1 structure includes a novel pivot and exposes a cluster of conserved tyrosine residues that are involved in Cdk binding but are sequestered in the beta-interchanged Cks homolog suc1 dimer structure [8].

Physical interactions of CKS1

• The CKS1 gene of Saccharomyces cerevisiae encodes a small essential protein shown to interact genetically and physically with the Cdc28 protein kinase [9].

Regulatory relationships of CKS1

• Cln2 and Cdc28 subunits coexpressed in baculovirus-infected insect cells fail to exhibit protein kinase activity towards multiple substrates in the absence of Cks1 [10].

Other interactions of CKS1

• The third, CKS1, encodes an 18K (K = 10(3) Mr) protein that has been shown to be a component of the Cdc28 protein kinase complex and is a homolog of the suc1+ product of fission yeast [11].
• Cks1-dependent proteasome recruitment and activation of CDC20 transcription in budding yeast [7].
• These included the known associated proteins Cdc28, Sic1 and Cks1 [12].

Analytical, diagnostic and therapeutic context of CKS1

• The product of cks1 is a 12 kDa polypeptide, which has 70% identity with human p9cks1 and 44% identity with fission yeast p13suc1.p12cks1 was detected in the three life-cycle stages of L. mexicana by immunoblotting [13].

References