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One important function of Aurora A in mitotic cells is to promote microtubule nucleation around the chromatin by phosphorylating NEDD1, and thereby to promote functional spindle assembly.
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The mice treated with small interfering (si) RNA targeting NEDD1 by the atelocollagen-mediated delivery system showed a significantly prolonged survival in a xenograft model of human gastric cancer.
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Data suggest that the NEDD1/gamma-tubulin interaction is finely tuned by multiple phosphorylation events in the S557-S574 region and is critical for spindle assembly.
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Nek9 phosphorylates NEDD1 on Ser377 driving its recruitment and thereby that of gamma-tubulin to the centrosome in mitotic cells.
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a direct interaction with NEDD1 regulates gamma-tubulin recruitment to the centrosome
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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.
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The NEED1 protein was characterized and its function in centriole duplication and spindle assembly determined.
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FAM29A promotes microtubule amplification via recruitment of the NEDD1-gamma-tubulin complex to the mitotic spindle.
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Data propose NEDD1 may be a promising target for controlling cell proliferation, in particular if targeted in combination with Plk1 inhibitors.
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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.