Disease relevance of CDC1

• In this region the herpesvirus proteins are most like a yeast cell division control protein, and least like the retrovirus protein-tyrosine kinases [1].

High impact information on CDC1

• A cis-acting hexamer element ACGCGT (an MluI restriction site) is responsible for coordinating transcriptional regulation of these genes at the G1/S phase boundary and we have identified a binding activity, DSC1, that recognizes these sequences in a cell-cycle-dependent manner [2].
• In Schizosaccharomyces pombe, this regulation is mediated by MCB elements that serve as binding sites for the MBF/DSC-1 complex [3].
• Mutations in CDC1 severely depolarize the actin cytoskeleton, and these mutations prevent late Golgi elements from being retained in the bud [4].
• In wild-type yeast, the disruption of BRY1 has no apparent phenotype, but under conditions where the activities of SBF and DSC1/MBF are reduced, BRY1 becomes essential [5].
• The transcription factors SBF and DSC1/MBF bind SCB and MCB promoter elements, respectively, and are essential for the cell cycle progression of Saccharomyces cerevisiae through the control of G1 cyclin gene expression [5].

Biological context of CDC1

• The phenotype of the mutant is caused by a single amino acid change (Gly149 to Arg) in the essential yeast gene CDC1 [6].
• One of the mutations isolated through this screen was found to affect the essential gene CDC1 [7].
• The deduced amino acid sequence showed homology to the Saccharomyces cerevisiae CDC1 protein, implicated in manganese homeostasis [8].
• The frost gene of Neurospora crassa is a homolog of yeast cdc1 and affects hyphal branching via manganese homeostasis [8].
• A yeast transcription factor bypassing the requirement for SBF and DSC1/MBF in budding yeast has homology to bacterial signal transduction proteins [5].

Anatomical context of CDC1

• Cdc1 and the vacuole coordinately regulate Mn2+ homeostasis in the yeast Saccharomyces cerevisiae [9].

Other interactions of CDC1

• An alternative model is that the p34CDC28/G1 cyclin complexes have several targets post-START, one being DSC1 and the others being as yet unidentified components of the pathways leading to CDC4 function, spindle pole body duplication and bud emergence [10].
• Previous studies have demonstrated a direct interaction between Pol3 and Cdc1, the B-subunit of the complex [11].

References