The polo-like kinase PLK1 phosphorylates NUDC on serine residues S274 and S326. PLK1-mediated phosphorylation of NUDC is required for both mitotic spindle formation and cytokinesis (Zhou et al. 2003). Interaction of NUDC with dynactin and dynein complexes is also important for its role in mitosis (Aumais et al. 2003). In interphase cells, NUDC is acetylated on lysine residue K39 by an unknown protein acetyl transferase. Deacetylation of NUDC, possibly by HDAC3, at the beginning of mitosis is required for mitotic progression. The interaction of NUDC with PLK1 does not depend on the acetylation status of NUDC (Chuang et al. 2013).
Caldwell, GA, Caldwell, KA, Lin, SH, Luo, W, Aumais, JP, Nishino, M, Williams, SN, Yu-Lee, LY
Aumais, JP, Liu, X, Zhou, T, Yu-Lee, LY, Erikson, RL
protein serine/threonine kinase activity of p-T210-PLK1 [cytosol]
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