Sasaki et al., Tokyo, Japan. In Cancer Sci, 28 Feb 2013
The mice treated with small interfering (si) RNA targeting NEDD1, which encodes a gamma-tubulin ring complex-binding protein, by the atelocollagen-mediated delivery system showed a significantly prolonged survival.
Pelletier et al., Toronto, Canada. In Cell Cycle, Nov 2012
We previously reported that CEP192 interacts with NEDD1, a protein that associates with the γ-tubulin ring complex (γ-TuRC) and regulates its phosphorylation status during mitosis.
Pelletier et al., Toronto, Canada. In J Cell Sci, Sep 2012
NEDD1 is a γ-TuRC-interacting protein whose depletion, although not affecting γ-TuRC stability, causes spindle defects similar to the inhibition of its core subunits, including γ-tubulin.
Hashimoto et al., Ikoma, Japan. In Plant J, Jul 2012
Functional fusions of GIP1a with green fluorescent protein (GFP) were used to purify GIP1a-containing complexes from Arabidopsis plants, which contained all the subunits (except NEDD1) previously identified in the Arabidopsis γ-tubulin complexes.
Rhee et al., Seoul, South Korea. In J Cell Biol, 2012
Phosphoresistant point mutants of PCNT did not recruit centrosomal proteins, such as CEP192, GCP-WD (γ-complex protein with WD repeats), γ-tubulin, Aurora A, and PLK1, into the centrosome during mitosis.
Lee et al., Bethesda, United States. In Proc Natl Acad Sci U S A, 2011
Mechanistically, we demonstrated that Cdc2-dependent phosphorylation on a γ-tubulin ring complex (γ-TuRC) recruitment protein, Nedd1/GCP-WD, at the previously uncharacterized S460 residue induces the Nedd1-Plk1 interaction.
Morrison et al., Galway, Ireland. In Mol Biol Cell, 2010
Using live-cell imaging of cells that express fluorescently tagged NEDD1/GCP-WD and proliferating cell nuclear antigen, we found that ionizing radiation (IR)-induced centrosome amplification can occur outside S phase.
Lüders et al., Barcelona, Spain. In Mol Biol Cell, 2010
In Drosophila, Xenopus, and humans large γ-tubulin ring complexes (γTuRCs) have been described, which have a characteristic open ring-shaped structure and are composed of a similar set of subunits, named γ-tubulin, GCPs 2-6, and GCP-WD in humans.
Kumar et al., Adelaide, Australia. In Cell Death Dis, 2009
Disrupting the centrosome in early-passage mouse embryonic fibroblasts by depletion of NEDD1 also resulted in centrosomal fragmentation and subsequent premature entry into senescence.
Data suggest that sequential phosphorylation of Nedd1 by Cdk1 and Plk1 plays a role in targeting gamma tubulin ring complex to the centrosome by promoting the interaction of Nedd1 with the gammaTuRC component gamma-tubulin, during mitosis.
Stearns et al., Stanford, United States. In Nat Cell Biol, 2006
GCP-WD (NEDD1) broadly mediates targeting of the gamma-tubulin ring complex to sites of microtubule nucleation and to the mitotic spindle, which is essential for spindle formation.