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Results revealed a function independent of its transcriptional activity, as TTF-1 (show NKX2-1 ELISA Kits) was found to interact with DDB1 and block its binding to CHK1 (show CHEK1 ELISA Kits), which in turn attenuated ubiquitylation and subsequent degradation of CHK1 (show CHEK1 ELISA Kits).
SIRT7 inhibits TR4 degradation by deacetylation of DDB1.
the c-Abl (show ABL1 ELISA Kits) non-receptor kinase phosphorylates DDB1 at residue Tyr (show TYR ELISA Kits)-316 to recruit a small regulatory protein, DDA1 (show DDA1 ELISA Kits), leading to increased substrate ubiquitination
knockdown of DCAF7 (show DCAF7 ELISA Kits) reduced the degradation of DNA ligase I (show LIG1 ELISA Kits) in response to inhibition of proliferation and replacement of ubiquitylated lysine residues reduced the in vitro ubiquitylation of DNA ligase I (show LIG1 ELISA Kits) by Cul4-DDB1 and DCAF7 (show DCAF7 ELISA Kits). In contrast, a different E3 ubiquitin ligase regulates FEN-1 (show FEN1 ELISA Kits) turnover.
This study presents the crystal structure of the DDB1-DCAF1-HIV-1-Vpr-uracil-DNA glycosylase (show UNG ELISA Kits) (cyclin U (show CCNO ELISA Kits)) complex.
Our data are consistent with the idea that the CUL4A (show CUL4A ELISA Kits)/B-DDB1-CRBN (show CRBN ELISA Kits) complex catalyses the polyubiquitination and thus controls the degradation of CLC-1 (show CLCN1 ELISA Kits) channels.
These results revealed a novel role of DDB in H3K56Ac deacetylation during early step of NER (show NR1H2 ELISA Kits) and the existence of active functional cross-talk between DDB-mediated damage recognition and H3K56Ac deacetylation.
The identification of Vpr mutants which associate with DCAF1 but only poorly with DDB1 suggests that DCAF1 is necessary but is not sufficient for the Vpr association with DDB1-containing E3 ligase complex.
Data support a model wherein DDB1 and DDB2 (show DDB2 ELISA Kits) cooperate to repress Bcl-2 (show BCL2 ELISA Kits) transcription. DDB2 (show DDB2 ELISA Kits) recognizes and binds to the Bcl-2 (show BCL2 ELISA Kits) P1 promoter, and HDAC1 (show HDAC1 ELISA Kits) is recruited through the DDB1 subunit associated with DDB2 (show DDB2 ELISA Kits) to deacetylate histone H3K9.
The study presents the crystal structure of human CRBN bound to DDB1 and the drug lenalidomide.
Bovine herpesvirus-1 VP8 interacts with DDB1 and is monoubiquitinated during infection.
These studies identify CUL4-DDB1 complex as a novel post-translational regulator of stem and progenitor maintenance and differentiation.
uncovered a novel biological role for CUL4A (show CUL4A ELISA Kits)-DDB1-CDT2 E3 ligase that regulates molecular circadian behaviors via promoting ubiquitination-dependent degradation of CRY1 (show CRY1 ELISA Kits)
UCH-L1 disrupts a complex between the DDB1-CUL4 ubiquitin ligase complex.
In a constructive process, pM27 recruits DDB1 to exploit ubiquitin ligase (show RNF123 ELISA Kits) complexes catalyzing the obstruction of the STAT2 (show STAT2 ELISA Kits)-dependent antiviral state of cells to permit viral replication.
Hepatocyte-specific deletion of DDB1 induces liver regeneration and tumorigenesis.
These results indicate that DDB1 plays an essential role in maintaining viability and genomic integrity of dividing cells.
DDB1 plays an important role in development by controlling levels of cell cycle regulators and thereby maintaining genomic stability.
Caenorhabditis elegans DDB-1 is required for the degradation of CDT-1 during S phase. DDB-1 interacts specifically with CUL-4 but not with other C. elegans cullins.
Data show that SKN-1 protein levels, nuclear accumulation, and activity are repressed by the WD40 repeat protein WDR-23, which interacts with the CUL-4/DDB-1 ubiquitin ligase to presumably target the transcription factor for proteasomal degradation.
The protein encoded by this gene is the large subunit (p127) of the heterodimeric DNA damage-binding (DDB) complex while another protein (p48) forms the small subunit. This protein complex functions in nucleotide-excision repair and binds to DNA following UV damage. Defective activity of this complex causes the repair defect in patients with xeroderma pigmentosum complementation group E (XPE) - an autosomal recessive disorder characterized by photosensitivity and early onset of carcinomas. However, it remains for mutation analysis to demonstrate whether the defect in XPE patients is in this gene or the gene encoding the small subunit. In addition, Best vitelliform mascular dystrophy is mapped to the same region as this gene on 11q, but no sequence alternations of this gene are demonstrated in Best disease patients. The protein encoded by this gene also functions as an adaptor molecule for the cullin 4 (CUL4) ubiquitin E3 ligase complex by facilitating the binding of substrates to this complex and the ubiquitination of proteins.
DDB p127 subunit
, DNA damage-binding protein 1
, DNA damage-binding protein a
, HBV X-associated protein 1
, UV-DDB 1
, UV-damaged DNA-binding factor
, UV-damaged DNA-binding protein 1
, XPE-binding factor
, xeroderma pigmentosum group E-complementing protein
, damage-specific DNA-binding protein 1
, damage-specific DNA binding protein 1, 127kDa
, DNA damage-binding protein 1-like
, DNA repair protein
, damage-specific DNA-binding protein, DNA repair
, damaged-DNA recognition protein 1
, damage specific DNA binding protein 1