Ask about this productRelated genes to: WDR55 antibody
- Gene:
- WDR55 NIH gene
- Name:
- WD repeat domain 55
- Previous symbol:
- -
- Synonyms:
- FLJ20195, FLJ21702
- Chromosome:
- 5q31.3
- Locus Type:
- gene with protein product
- Date approved:
- 2005-02-24
- Date modifiied:
- 2019-03-21
Related products to: WDR55 antibody
Related articles to: WDR55 antibody
- We report an enantioselective protein affinity selection mass spectrometry screening approach (E-ASMS) that enables the detection of weak binders, informs on selectivity, and generates orthogonal confirmation of binding. After method development with control proteins, we screen 31 human proteins against a designed library of 8,217 chiral compounds. We identify 16 binders to 12 targets, including many proteins predicted to be "challenging to ligand", and confirm their interactions through orthogonal biophysical assays. Seven binders to six targets display enantioselective binding, with K values ranging from 3 to 20 µM. Binders for four targets (DDB1, WDR91, WDR55, and HAT1) are selected for in-depth characterization using X-ray crystallography. In all four cases, the mechanisms underlying enantioselectivity are readily explained. These results demonstrate that E-ASMS enables the identification and characterization of selective and weakly binding ligands for novel protein targets with unprecedented throughput and sensitivity. - Source: PubMed
Publication date: 2025/12/17
Wang XiaoyunSun JianxianAhmad ShabbirYang DiwenLi FenglingChan U HangZeng HongSimoben Conrad VGreen Stuart RSilva MadhushikaHouliston ScottDong AipingBolotokova AlbinaGibson ElisaKutera MariaGhiabi PegahKondratov IvanMatviyuk TetianaChuprina AlexanderMavridi DanaiLenz ChristopherJoerger Andreas CBrown Benjamin DHeath Richard BYue Wyatt WRobbie Lucy KBeyett Tyler SMüller SusanneKnapp StefanOwen Dafydd RHarding RachelSchapira MatthieuBrown Peter JSanthakumar VijayaratnamAckloo SuzanneArrowsmith Cheryl HEdwards Aled MPeng HuiHalabelian Levon - We report an enantioselective protein affinity selection mass spectrometry screening approach (E-ASMS) that enables the detection of weak binders, informs on selectivity, and generates orthogonal confirmation of binding. After method development with control proteins, we screened 31 human proteins against a designed library of 8,210 chiral compounds. 16 binders to 12 targets, including many proteins predicted to be "challenging to ligand", were discovered and confirmed in orthogonal biophysical assays. 7 binders to 6 targets bound in an enantioselective manner, with values ranging from 3 to 20 μM. Binders for four targets (DDB1, WDR91, WDR55, and HAT1) were selected for in-depth characterization using X-ray crystallography. In all four cases, the mechanism for enantioselectivity was readily explained. We conclude E-ASMS can be used to identify and characterize selective and weakly-binding ligands for novel protein targets with unprecedented throughput and sensitivity. - Source: PubMed
Publication date: 2025/04/25
Wang XiaoyunSun JianxianAhmad ShabbirYang DiwenLi FenglingChan U HangZeng HongSimoben Conrad VGreen Stuart RSilva MadhushikaHouliston ScottDong AipingBolotokova AlbinaGibson ElisaKutera MariaGhiabi PegahKondratov IvanMatviyuk TetianaChuprina AlexanderMavridi DanaiLenz ChristopherJoerger Andreas CBrown Benjamin DHeath Richard BYue Wyatt WRobbie Lucy KBeyett Tyler SMüller SusanneKnapp StefanHarding RachelSchapira MatthieuBrown Peter JSanthakumar VijayaratnamAckloo SuzanneArrowsmith Cheryl HEdwards Aled MPeng HuiHalabelian Levon - Despite plant's ability to adapt and withstand challenging environments, drought poses a severe threat to their growth and development. Although pigeon pea is already quite resistant to drought, the prolonged dehydration induced by the aberrant climate poses a serious threat to their survival and productivity. - Source: PubMed
Publication date: 2023/11/20
Pahal SumanSrivastava HarshaSaxena SwatiTribhuvan Kishor UKaila TanviSharma SandhyaGrewal SapnaSingh Nagendra KGaikwad Kishor - WDR54 is a member of the WD40 repeat (WDR) domain-containing protein family that was recently identified as a novel oncogene in colorectal cancer. However, the molecular mechanism of WDR54 and its functional association with other molecules related to tumor cell growth are unknown. Here, we show that WDR54 can be cross-linked by the action of transglutaminase (TG) 2, which enhances the activation of EGF receptor-mediated signaling pathway. The most carboxyl-terminal WD domain was required for cross-linking. In addition, lysine 280 in WDR54, also in this WD domain, was an important residue for both cross-linking and ubiquitination. Cross-linked WDR54 was found in vesicles aggregated at the plasma membrane. The activated EGF receptor was co-localized with this vesicle, and the internalization of the EGF receptor into the cytosol was sustained. As a result, Erk activity in response to EGF stimulation was enhanced. Furthermore, the growth of the cells lacking WDR54 expression generated by genome editing was delayed compared with that in wild-type cells. Because TG2 is also has been proposed to activate the EGF receptor-signaling and proliferation of tumor cells, WDR54 might have a functional relationship with the EGF receptor and TG2. Our study on the mechanism of biological function of WDR54 may provide rationale for the design and development of a cancer drug based on inhibiting the post-translational modification of this oncogene product. - Source: PubMed
Publication date: 2018/11/17
Maeda AkaneNishino TasukuMatsunaga RyotaYokoyama AtsushiSuga HiroshiYagi ToshikiKonishi Hiroaki - The CULLIN family of E3 ubiquitin ligases are important regulators of plant development and function. A newly identified class of CULLIN4-RING-E3 ligases (CRL4s) interacts with substrate receptors referred to as DDB1-CUL4 ASSOCIATED FACTORS (DCAFs) via a DDB1 linker protein. We have previously reported that the WD40 protein WDR55 interacts with DDB1A and is thus a putative DCAF. Mutants of WDR55 are embryo lethal, suggesting that a DDB1(WDR55) complex could regulate embryo and endosperm development. Here we report that a weak allele homozygous for wdr55 display pleiotropic phenotypes in the seedling and adult stages, suggesting a novel regulatory role for WDR55 in vegetative development. - Source: PubMed
Publication date: 2013/06/18
Bjerkan Katrine NGrini Paul E