PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination - Test2 - elhamkhani - TriplyDB

PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination

PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination

http://www.wikidata.org/entity/Q28291192

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Cdt1 associates dynamically with chromatin throughout G1 and recruits Geminin onto chromatin CRL4(Cdt2) E3 ubiquitin ligase monoubiquitinates PCNA to promote translesion DNA synthesis Selective ubiquitylation of p21 and Cdt1 by UBCH8 and UBE2G ubiquitin-conjugating enzymes via the CRL4Cdt2 ubiquitin ligase complex.DTL/CDT2 is essential for both CDT1 regulation and the early G2/M checkpoint PCNA-dependent regulation of p21 ubiquitylation and degradation via the CRL4Cdt2 ubiquitin ligase complex.Prevention of DNA re-replication in eukaryotic cells Replication licensing and cancer--a fatal entanglement?Intrinsic negative cell cycle regulation provided by PIP box- and Cul4Cdt2-mediated destruction of E2f1 during S phase Endoreplication: polyploidy with purpose Mechanisms to control rereplication and implications for cancer.DNA damage induces Cdt1 proteolysis in fission yeast through a pathway dependent on Cdt2 and Ddb1 Mcm10 and And-1/CTF4 recruit DNA polymerase alpha to chromatin for initiation of DNA replication Ring of Change: CDC48/p97 Drives Protein Dynamics at Chromatin Genomic instability in cancer.Sequential replication-coupled destruction at G1/S ensures genome stability.Structure of the Cdt1 C-terminal domain: Conservation of the winged helix fold in replication licensing factors Quaternary structure of the human Cdt1-Geminin complex regulates DNA replication licensing Interaction between PCNA and diubiquitinated Mcm10 is essential for cell growth in budding yeast Functional dissection of the catalytic carboxyl-terminal domain of origin recognition complex subunit 1 (PfORC1) of the human malaria parasite Plasmodium falciparum Distinct and overlapping functions of the cullin E3 ligase scaffolding proteins CUL4A and CUL4B CDK inhibitor p21 is degraded by a proliferating cell nuclear antigen-coupled Cul4-DDB1Cdt2 pathway during S phase and after UV irradiation A novel function of CRL4(Cdt2): regulation of the subunit structure of DNA polymerase δ in response to DNA damage and during the S phase SET8 is degraded via PCNA-coupled CRL4(CDT2) ubiquitylation in S phase and after UV irradiation The tail that wags the dog: p12, the smallest subunit of DNA polymerase δ, is degraded by ubiquitin ligases in response to DNA damage and during cell cycle progression Cell cycle-regulated protein abundance changes in synchronously proliferating HeLa cells include regulation of pre-mRNA splicing proteins USP37 deubiquitinates Cdt1 and contributes to regulate DNA replication Two subunits of human ORC are dispensable for DNA replication and proliferation.Inactivation of the CRL4-CDT2-SET8/p21 ubiquitylation and degradation axis underlies the therapeutic efficacy of pevonedistat in melanoma.CRL4Cdt2 E3 ubiquitin ligase and proliferating cell nuclear antigen (PCNA) cooperate to degrade thymine DNA glycosylase in S phase 14-3-3 proteins play a role in the cell cycle by shielding cdt2 from ubiquitin-mediated degradation Degradation of p12 subunit by CRL4Cdt2 E3 ligase inhibits fork progression after DNA damage.Regulation of TGF-β signaling, exit from the cell cycle, and cellular migration through cullin cross-regulation: SCF-FBXO11 turns off CRL4-Cdt2.CRL1-FBXO11 promotes Cdt2 ubiquitylation and degradation and regulates Pr-Set7/Set8-mediated cellular migration.Stress-stimulated mitogen-activated protein kinases control the stability and activity of the Cdt1 DNA replication licensing factor NEDD8-targeting drug MLN4924 elicits DNA rereplication by stabilizing Cdt1 in S phase, triggering checkpoint activation, apoptosis, and senescence in cancer cells CRL4(Cdt2) regulates cell proliferation and histone gene expression by targeting PR-Set7/Set8 for degradation CRL4Cdt2: master coordinator of cell cycle progression and genome stability Acetylation/deacetylation modulates the stability of DNA replication licensing factor Cdt1.DDB1 maintains genome integrity through regulation of Cdt1 The ubiquitin system, disease, and drug discovery.

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P2860

PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination

http://www.wikidata.org/entity/Q28291192

description

2006 nî lūn-bûn

@nan

2006 թուականի Մարտին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի մարտին հրատարակված գիտական հոդված

@hy

2006年の論文

@ja

2006年論文

@yue

2006年論文

@zh-hant

2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

@zh-tw

2006年论文

@wuu

name

PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination

@ast

PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination

@en

PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination

@nl

type

label

PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination

@ast

PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination

@en

PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination

@nl

prefLabel

PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination

@ast

PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination

@en

PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination

@nl

P1433

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P1476

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P2093

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P2860

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P921

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P3181

P356

P1433

Journal of Biological Chemistry

P1476

PCNA is a cofactor for Cdt1 degradation by CUL4/DDB1-mediated N-terminal ubiquitination

@en

P2093

Emily E Arias

http://www.w3.org/2001/XMLSchema#string

Jong Hoon Park

http://www.w3.org/2001/XMLSchema#string

Takeshi Senga

http://www.w3.org/2001/XMLSchema#string

Umasundari Sivaprasad

http://www.w3.org/2001/XMLSchema#string

Wenge Zhu

http://www.w3.org/2001/XMLSchema#string

P2860

Inhibition of eukaryotic DNA replication by geminin binding to Cdt1

Cdt1 phosphorylation by cyclin A-dependent kinases negatively regulates its function without affecting geminin binding

Regulation of DNA replication and repair proteins through interaction with the front side of proliferating cell nuclear antigen

Rereplication by depletion of geminin is seen regardless of p53 status and activates a G2/M checkpoint

N-Terminal ubiquitination of extracellular signal-regulated kinase 3 and p21 directs their degradation by the proteasome

Loss of Geminin induces rereplication in the presence of functional p53

DNA replication in eukaryotic cells

The SCF(Skp2) ubiquitin ligase complex interacts with the human replication licensing factor Cdt1 and regulates Cdt1 degradation

Radiation-mediated proteolysis of CDT1 by CUL4-ROC1 and CSN complexes constitutes a new checkpoint

The human licensing factor for DNA replication Cdt1 accumulates in G1 and is destabilized after initiation of S-phase

P304

6246-6252

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P3181

1891538

http://www.w3.org/2001/XMLSchema#string

P356

10.1074/JBC.M512705200

http://www.w3.org/2001/XMLSchema#string

P407

P433

10

http://www.w3.org/2001/XMLSchema#string

P478

281

http://www.w3.org/2001/XMLSchema#string

P50

Johannes C Walter

P577

2006-01-09T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P698

16407252

http://www.w3.org/2001/XMLSchema#string

P921

protein ubiquitination