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ATM (show ATM Proteins) silencing induced partial reduction in levels of Skp2, a component of SCF (show KITLG Proteins)(Skp2) ubiquitin ligase that controls Cdt1 degradation.
FBXO31 (show FBXO5 Proteins) interacts with Cdt1 and regulates the degradation of Cdt1 in G2 phase.
Protein levels of Geminin (show GMNN Proteins) and Cdt1 are tightly regulated through the cell cycle, and the Cdt1-Geminin (show GMNN Proteins) complex likely acts as a molecular switch that can enable or disable the firing of each origin of replication.
These results demonstrate an important role for Cdt1 in human papillomavirus E7-induced rereplication and shed light on mechanisms by which human papillomavirus induces genomic instability.
ATR (show ANTXR1 Proteins), activated after DNA damage, phosphorylates Cdt2 (show DTL Proteins) and promotes the rapid degradation of Cdt1 after UV irradiation in the G1 phase of the cell cycle.
A lethal phenotype was seen in four individuals with compound heterozygous CDT1 mutations
results support the conclusion that Cdt1 binding to Hec1 (show NDC80 Proteins) is essential for an extended Ndc80 (show NDC80 Proteins) configuration and stable kinetochore-microtubule attachment
Genes in the erythroid differentiation and cell cycle regulation pathways influence interindividual variation in RBC (show CACNA1C Proteins) indices. Our results provide insights into the molecular basis underlying variation in RBC (show CACNA1C Proteins) traits.
FOXO3 (show FOXO3 Proteins) is a binding partner of Cdt1.
The over-expression of geminin (show GMNN Proteins) and cdt1 may play an important role in pathogenesis of acute leukemia.
This study reveals a conserved new regulatory Cdt1 domain crucial for proper DNA licensing activity.
Structure and mutagenesis studies of the C-terminal region of licensing factor Cdt1 enable the identification of key residues for binding to replicative helicase Mcm proteins.
Determined the structures of mCdt1CS (mCdt1C_small; residues 452 to 557) and mCdt1CL (mCdt1C_large; residues 420 to 557) using X-ray crystallography and NMR. This study reveals that Cdt1 is formed with a tandem repeat of the winged helix domain.
Cdt1 function is negatively regulated by the Cdk (show CDK4 Proteins) phosphorylation independent of geminin (show GMNN Proteins) binding
crystal structure of the mouse geminin (show GMNN Proteins)-Cdt1 complex using tGeminin (residues 79-157, truncated geminin (show GMNN Proteins)) and tCdt1 (residues 172-368, truncated Cdt1)
In situ hybridization and immunohistochemistry localize Cdt1 as well as geminin (show GMNN Proteins) to the proliferative compartment of the developing mouse gut (show GUSB Proteins) epithelium
Cdt1 expression characterizes progenitor cells in G1 phase
These results suggested that, at least in vitro, oleic acid-containing cell membranes of the lipid bilayer inhibit Cdt1-geminin (show GMNN Proteins) complex formation by binding to Cdt1 and thereby liberating Cdt1 from inhibition by geminin (show GMNN Proteins).
DNA binding and helicase activities of Mcm4 (show MCM4 Proteins)/6/7 are significantly stimulated by Cdt1
PcG complex 1, involving Rae28 and Cdt1, supports the activity of hematopoietic stem cells by enhancing cycling capability and hematopoietic activity through direct regulation of Geminin (show GMNN Proteins)
These findings suggested that excess Cdt1 suppressed the progression of replication forks.
Dynamic interactions of high Cdt1 and geminin (show GMNN Proteins) levels regulate S phase in early Xenopus embryos.
p97 (show vcp Proteins) is an essential regulator of DNA damage-dependent CDT1 destruction
CDC-48/p97 (show vcp Proteins) coordinates CDT-1 degradation with GINS chromatin dissociation to ensure faithful DNA replication
Loading of geminin (show GMNN Proteins) onto chromatin requires Cdt1, suggesting that geminin (show GMNN Proteins) is targeted at replication origins.
results allow us to build a comprehensive model of how re-replication of DNA is prevented in Xenopus, with Cdt1 regulation being the key feature
Removal of Cdt1 from chromatin and its nuclear exclusion in G2 is critical in regulating licensing and limiting DNA replication in S phase to only one round.
Cdt1 and DDB1 (show DDB1 Proteins) interact in extracts, and DDB1 (show DDB1 Proteins) chromatin loading is dependent on the binding of Cdt1 to PCNA (show PCNA Proteins), which indicates that PCNA (show PCNA Proteins) docking activates the pre-formed Cdt1-Cul4(DDB1 (show DDB1 Proteins)) ligase complex.
These results suggest a model in which the MCM2-7 (show MCM2 Proteins) helicase is loaded onto chromatin by a Cdt1-geminin (show GMNN Proteins) complex, which is inactivated upon origin firing by binding additional geminin (show GMNN Proteins).
Cdt1, with its two opposing regulatory binding factors MCM9 (show MCM9 Proteins) and geminin (show GMNN Proteins), appears to be a major platform on the pre-replication complexes to integrate cell-cycle signals.
The protein encoded by this gene is involved in the formation of the pre-replication complex that is necessary for DNA replication. The encoded protein can bind geminin, which prevents replication and may function to prevent this protein from initiating replication at inappropriate origins. Phosphorylation of this protein by cyclin A-dependent kinases results in degradation of the protein.
chromatin licensing and DNA replication factor 1
, DNA replication factor Cdt1-like
, DNA replication factor Cdt1
, Double parked, Drosophila, homolog of
, double parked homolog
, retroviral insertion site 2 protein
, retroviral integration site 1
, retroviral integration site 2
, DNA replication factor