Details

Autor(en) / Beteiligte

• Weiderhold, Kimberly N
• Fadri-Moskwik, Maria
• Pan, Jing
• Nishino, Michiya
• Chuang, Carol
• Deeraksa, Arpaporn
• Lin, Sue-Hwa
• Yu-Lee, Li-Yuan
• Prigent, Claude

Titel

Dynamic Phosphorylation of NudC by Aurora B in Cytokinesis

Ist Teil von

• PloS one, 2016-04, Vol.11 (4), p.e0153455-e0153455

Ort / Verlag

United States: Public Library of Science

Erscheinungsjahr

2016

Link zum Volltext

Quelle

EZB Free E-Journals

Beschreibungen/Notizen

• Nuclear distribution protein C (NudC) is a mitotic regulator that plays a role in cytokinesis. However, how NudC is regulated during cytokinesis remains unclear. Here, we show that NudC is phosphorylated by Aurora B, a kinase critical for cell abscission. NudC is co-localized with Aurora B at the midbody and co-immunoprecipitated with Aurora B in mitosis. Inhibition of Aurora B by ZM447439 reduced NudC phosphorylation, suggesting that NudC is an Aurora B substrate in vivo. We identified T40 on NudC as an Aurora B phosphorylation site. NudC depletion resulted in cytokinesis failure with a dramatic elongation of the intercellular bridge between daughter cells, sustained Aurora B activity at the midbody, and reduced cell abscission. These cytokinetic defects can be rescued by the ectopic expression of wild-type NudC. Reconstitution with T40A phospho-defective NudC was found to rescue the cytokinesis defect. In contrast, reconstitution with the T40D phospho-mimetic NudC was inefficient in supporting the completion of cytokinesis. These results suggest that that dynamic phosphorylation of NudC by Aurora B regulates cytokinesis.