Disease relevance of WDR1

• Therefore, in the present study, we undertook to determine the distribution of WDR1 within PC12 pheochromocytoma cells (PC12 cells) using light and electron microscopic techniques [1].
• Rapid actin monomer-insensitive depolymerization of Listeria actin comet tails by cofilin, coronin, and Aip1 [2].
• The orthologous human gene (FLJ12973), is expressed ubiquitously and encodes a WD-repeat protein with structural similarity to DDB2, the small subunit of the xeroderma pigmentosum XP-E complex [3].
• Structural Organization of the WD repeat protein-encoding gene HIRA in the DiGeorge syndrome critical region of human chromosome 22 [4].
• Endonuclein is a cell cycle regulated WD-repeat protein that is up-regulated in adenocarcinoma of the pancreas [5].

Psychiatry related information on WDR1

• Badia-Elder; (3) The gut peptide cholecystokinin controls alcohol intake in Sardinian alcohol-preferring rats, by Nori Geary and Maurizio Massi; and (4) Hypothalamic galanin: a possible role in excess alcohol drinking, by Sarah F [6].

High impact information on WDR1

• The predicted product of AAAS, ALADIN (for alacrima-achalasia-adrenal insufficiency neurologic disorder), belongs to the WD-repeat family of regulatory proteins, indicating a new disease mechanism involved in triple-A syndrome [7].
• FAN, a novel WD-repeat protein, couples the p55 TNF-receptor to neutral sphingomyelinase [8].
• We report the cloning of the CSA cDNA, which can encode a WD repeat protein [9].
• Here we demonstrate that Tip targets a lysosomal protein p80, which consists of an N-terminal WD repeat domain and a C-terminal coiled-coil domain [10].
• We show here that Gemin5, a 170 kDa WD-repeat protein, is the snRNA binding protein of the SMN complex [11].

Chemical compound and disease context of WDR1

• The rats were fed with 4 g of the control diet or 4 g of the nori diet containing a standard dioxin solution (233 ngTEQ/kg of body weight) for five consecutive days [12].

Biological context of WDR1

• The WDR1 gene was mapped to human chromosome 4, between 22 and 24 cM from the telomere of 4p [13].
• Molecular cloning, expression analysis, and chromosome mapping of WDR6, a novel human WD-repeat gene [14].
• The WD-repeat proteins are found in all eukaryotes and play an important role in the regulation of a wide variety of cellular functions such as signal transduction, transcription, and proliferation [14].
• Conversely, an amino acid change (E to K) in the sixth WD repeat of UNC-37 is a strong suppressor of unc-37(e262) and of specific unc-4 missense mutations [15].
• In addition, we show that the WD repeat domains of UNC-37 and of the human homolog, TLE1, are functionally interchangeable in VA motor neurons which suggests that this highly conserved protein domain may also specify motor neuron identity and synaptic choice in more complex nervous systems [15].

Anatomical context of WDR1

• The chick WDR1 gene is expressed at higher levels in the chick basilar papilla after acoustic overstimulation [13].
• However, the peak frequency of WDR2 neurons often reached a plateau below 47 degrees C. Both WDR1 and WDR2 neurons had receptive fields that encompassed one or two divisions of the trigeminal nerve [16].
• We carried out a direct observation of actin filament severing/disassembly assay and found that phosphorylated cofilin still somewhat severs/disassembles actin filaments and that AIP1/WDR1 effaces this in vitro [17].
• Wdr5, a novel WD repeat protein, regulates osteoblast and chondrocyte differentiation in vivo [18].
• RTG-dependent mitochondria to nucleus signaling is negatively regulated by the seven WD-repeat protein Lst8p [19].

Associations of WDR1 with chemical compounds

• The WD repeat scaffolding protein RACK1 can mediate integration of the insulin-like growth factor I receptor (IGF-IR) and integrin signaling in transformed cells [20].
• Pak1 phosphorylates p41-Arc on threonine 21 in the first WD repeat, and its mutation has functional implications in vivo [21].
• The substituted glycine is located in the WD-repeat domain of Smu1 [22].
• A deduced Thermomonospora curvata protein containing serine/threonine protein kinase and WD-repeat domains [23].
• More than a 100-fold increase in immunoblot signals of laser-microdissected inclusion bodies with an excessive aggregation property by oligomeric actin interacting protein 2/D-lactate dehydrogenase protein 2 [24].

Physical interactions of WDR1

• Here, we show that SUZ12 interacts with WD-repeat protein MEP50 in vitro and in vivo [25].

Regulatory relationships of WDR1

• A strategy of mutagenesis followed by yeast two-hybrid assay was used to determine the sites on the WD-repeat protein Receptor for Activated C Kinase 1 (RACK1) necessary for it to interact with the cAMP-specific phosphodiesterase isoform PDE4D5 [26].
• The WD-repeat protein called p55(CDC)(Cdc20) directly binds to and activates APC/C [27].

Other interactions of WDR1

• Association of Polycomb group SUZ12 with WD-repeat protein MEP50 that binds to histone H2A selectively in vitro [25].
• Triple A syndrome is caused by mutations in AAAS, a new WD-repeat protein gene [28].
• Cloning and expression analysis of a novel WD repeat gene, WDR3, mapping to 1p12-p13 [29].
• A highly conserved human gene encoding a novel member of WD-repeat family of proteins (WDR13) [30].
• A cDNA fragment originally identified in U-937 cells as a vitamin D(3)-regulated gene is here designated the glutamate-rich WD-repeat (GRWD1) gene [31].

Analytical, diagnostic and therapeutic context of WDR1

• Double immunocytochemistry clearly showed that WDR1 immunoreactivities (IRs) were co-localized with anti-actin antibody, suggesting the involvement of WDR1 in actin dynamics [1].
• We identified a novel WD-repeat protein, recently designated Morg1 (MAPK organizer 1), by screening a cDNA library with yeast two-hybrid assays [32].
• Site-directed mutagenesis suggested that Aip1p has two actin binding sites, the primary actin binding site lies on the edge of its N-terminal beta-propeller and a secondary actin binding site lies in a comparable location on its C-terminal beta-propeller [33].
• A genetic dissection of Aip1p's interactions leads to a model for Aip1p-cofilin cooperative activities [33].
• Here we demonstrate that the far-UV circular dichroism spectrum of the WD repeat-containing RACK1 protein shows an unusual positive ellipticity at 229 nm, which in other proteins of the WD family has been attributed to surface tryptophans that are quenchable by N-bromosuccinimide (NBS) [34].

References