PLK1 phosphorylates NUDC

Stable Identifier
Reaction [transition]
Homo sapiens
Regulation of NUDC by phosphorylation
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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).

Literature References
PubMed ID Title Journal Year
12852857 A role for Plk1 phosphorylation of NudC in cytokinesis

Zhou, T, Aumais, JP, Liu, X, Yu-Lee, LY, Erikson, RL

Dev Cell 2003
12679384 Role for NudC, a dynein-associated nuclear movement protein, in mitosis and cytokinesis

Aumais, JP, Williams, SN, Luo, W, Nishino, M, Caldwell, KA, Caldwell, GA, Lin, SH, Yu-Lee, LY

J Cell Sci 2003
Catalyst Activity

protein serine/threonine kinase activity of p-T210-PLK1 [cytosol]

Orthologous Events
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