DDA1 (aa32_42)
- Known as:
- DDA1 (aa32_42)
- Catalog number:
- Y214488
- Product Quantity:
- 200ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- DDA1 (aa32_42)
Related genes to: DDA1 (aa32_42)
- Gene:
- DDA1 NIH gene
- Name:
- DET1 and DDB1 associated 1
- Previous symbol:
- C19orf58
- Synonyms:
- PCIA1, MGC2594
- Chromosome:
- 19p13.11
- Locus Type:
- gene with protein product
- Date approved:
- 2006-08-22
- Date modifiied:
- 2014-11-19
Related products to: DDA1 (aa32_42)
anti-CDw218a / IL18R1 (aa32-329)ApoC-I proteinApoC-I protein, Native & Recombinant ProteinsBos taurus,Bovine,DDA1,DET1- and DDB1-associated protein 1Bovine DET1 and DDB1 associated 1 (DDA1) ELISA kit, Species Bovine, Sample Type serum, plasmaBovine DET1- and DDB1-associated protein 1(DDA1) ELISA kitBovine DET1- and DDB1-associated protein 1(DDA1) ELISA kit SpeciesBovineC19orf58,DDA1,DET1- and DDB1-associated protein 1,Homo sapiens,Human,PCIA1,PCIA-1,Placenta cross-immune reaction antigen 1Chicken DET1 and DDB1 associated 1 (DDA1) ELISA kit, Species Chicken, Sample Type serum, plasmaChicken DET1- and DDB1-associated protein 1(DDA1) ELISA kitChicken DET1- and DDB1-associated protein 1(DDA1) ELISA kit SpeciesChickenChicken,DDA1,DET1- and DDB1-associated protein 1,Gallus gallus,RCJMB04_13o6DCX Gene doublecortinDda1DDA1 Related articles to: DDA1 (aa32_42)
- Ubiquitin modifications regulate fundamental cellular activities by modulating protein stability and function. The ubiquitin ligase COP1, which is present across species from plants to humans, plays a crucial role in the ubiquitination of developmental transcription factors. While COP1 can function independently, it can also be incorporated into CULLIN4-RING ubiquitin ligase (CRL4) complexes through the DET1 adaptor protein. Despite its biological significance, the structural and functional mechanisms of COP1 and DET1-containing complexes remains poorly understood. Here we present the cryo-electron microscopy structures of human COP1 in complex with DDB1-DDA1-DET1 and Ube2e2, revealing an inactive stacked assembly state. Co-expression with COP1 substrates including c-Jun or ETS2 disrupts this configuration, inducing a conformational rearrangement into a distinct dimeric state that allows substrate access. Structural modelling identifies the spatial organization of COP1 WD40 domains where substrate recruits. DET1 serves as a structural scaffold, bridging COP1 and Ube2e2 to initiate potential ubiquitin addition on substrates, while DDB1 recruits the CULLIN4-RBX1 complex to facilitate Ube2d3-mediated ubiquitin chain elongation. These results reveal the dynamic interplay between the structural states of the CRL4 E3 ligase complex and its substrate specific activation mechanism, offering mechanistic insights into ubiquitination regulation and a basis for future studies on E3 ligase dynamics. - Source: PubMed
Publication date: 2026/01/15
Wang ShanTeng FeiStjepanovic GoranRao FengSu Ming-Yuan - Understanding protein-protein interactions (PPIs) in planta is essential for deciphering the molecular mechanisms underlying plant development and responses to environmental stresses. Here, we demonstrate the application of the split firefly luciferase complementation assay (SplitLUC) using a cooled charge-coupled device (CCD)-based plant imaging system and a microplate reader to detect and quantify PPIs in planta. As an example, we investigated the previously reported interaction between DET1- and DDB1-ASSOCIATED 1 (DDA1), a component of the CULLIN4 (CUL4)-E3 ubiquitin ligase complex, and PYR1-like 8 (PYL8), a known substrate of the same complex. Co-infiltration of Agrobacterium strains carrying DDA1-nLUC and cLUC-PYL8 constructs resulted in a robust luminescent signal upon addition of D-luciferin, which was visualised and quantified using the NightSHADE evo Plant Imaging System. Control combinations lacking either fusion partner or containing only empty vectors did not produce detectable luminescence, confirming the specificity of the interaction. To account for infiltration efficiency and variability in transgene expression, the luminescence values were normalised against fluorescence from co-infiltrated TagRFP, measured using a Tecan Spark microplate reader. This normalisation strategy effectively mitigated leaf-to-leaf variation in luminescence signals and demonstrated that the SplitLUC assay, when combined with fluorescence-based normalisation, provides a robust and reliable quantitative method for studying PPIs in planta. We propose that this approach is well-suited for investigating weaker interactions, assessing the influence of additional (bridge) proteins, and mapping interaction domains within the proteins of interest. - Source: PubMed
Publication date: 2025/12/11
Liu QianweiKembügler RainerFelipe FrancescPonnu Jathish - Targeted protein degradation (TPD) leverages the ubiquitin-proteasome system to eliminate disease-causing proteins via E3 ligases. To date, the field is limited to utilizing a few of the over 600 human E3 ligases. To expand this repertoire, we conducted structural and functional validation of DDB1 (Damage-specific DNA binding protein 1) and Cullin-associated factor (DCAF)2 (DTL/CDT2), a Cullin4-RING ligase substrate adaptor implicated in DNA damage response and cancer, as a novel E3 for TPD. Cryoelectron microscopy (cryo-EM) structures of the DCAF2:DDB1:DDA1 complex (3.3 Å), a ligand bound complex (3.1 Å), and a ternary complex with a covalent proteolysis-targeting chimera (PROTAC) and BRD4 (3.4 Å) reveal PROTAC-mediated substrate recruitment. Using covalent bifunctional tool compounds engaging residue C141 in the WD40 domain, we demonstrate robust ubiquitination in biochemical assays and cellular TPD using the COFFEE (covalent functionalization followed by E3 electroporation) method. These findings position DCAF2 as a promising E3 adaptor for PROTAC strategies and identify C141 as a relevant site for future PROTAC discovery. - Source: PubMed
Publication date: 2025/10/03
McMahon Evan JCioffi Alexander GVisperas Patrick RLin YueqingShaghafi MichaelDaczkowski Courtney MHermann Johannes CEverley Robert ANeve Richard MErlanson Daniel AWebster Kevin RNarayan VikramWang Weiru - Caffeine is commonly consumed at night by shift workers and military personnel to promote alertness, yet its adverse effects remain underexplored. Here, we show that nighttime caffeine intake impairs inhibitory control in , resulting in impulsive motor behavior, with females more sensitive than males. This effect is independent of hyperactivity or sleep loss, as walking speed was unchanged and artificial sleep deprivation via light or mechanical stimulation did not elicit similar deficits. Notably, daytime caffeine intake did not impair inhibitory control, highlighting a circadian gating of caffeine's impact. Mechanistically, we show that dopamine signaling mediates this effect. Reduced dopamine synthesis, silencing of protocerebral anterior medial (PAM) dopaminergic neurons, or altered dopamine transporter activity attenuated or exacerbated impulsivity. Targeted manipulations identified the dopamine D1 receptor (dDA1/Dop1R1) in the mushroom body (MB) α/β and γ lobes as essential for this effect, with γ-lobe neurons exhibiting heightened sensitivity. These findings uncover a circadian- and dopamine-dependent mechanism. - Source: PubMed
Publication date: 2025/07/24
Saldes Erick BenjaminSabandal Paul RafaelHan Kyung-An - Caffeine is commonly consumed at night by shift workers and military personnel for its wake-promoting effect, yet its adverse effects on behavior remain underexplored. Here, we show that nighttime caffeine intake impairs inhibitory control in , resulting in impulsive motor behavior, with females more sensitive than males. This effect is independent of hyperactivity or sleep loss, as walking speed was unchanged, and artificial sleep deprivation via light or mechanical stimulation did not elicit similar deficits. Notably, daytime caffeine feeding did not impair inhibitory control, highlighting a circadian gating of caffeine's behavioral impact. Mechanistically, we identify dopamine signaling as a key mediator of caffeine-induced impulsivity. Reduced dopamine synthesis ( ), silencing of PAM dopaminergic neurons, or altered dopamine transporter activity ( ) attenuated or exacerbated caffeine-induced impulsivity. Targeted manipulations identified the dopamine D1 receptor (dDA1/Dop1R1) in the mushroom body (MB) α/β and γ lobes as essential for this effect, with γ-lobe neurons exhibiting heightened sensitivity. These findings reveal a circadian- and dopamine-dependent mechanism through which nighttime caffeine impairs behavioral inhibition. - Source: PubMed
Publication date: 2025/06/13
Saldes Erick BenjaminSabandal Paul RafaelHan Kyung-An