PLK1 phosphorylates NUDC

Stable Identifier
R-HSA-156682
Type
Reaction [transition]
Species
Homo sapiens
Compartment
Synonyms
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
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
protein serine/threonine kinase activity of p-T210-PLK1 [cytosol]
Physical Entity
Activity
Orthologous Events
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Reviewed
Created