NEK6 and NEK7 phosphorylate EML4

Stable Identifier
R-HSA-9648089
Type
Reaction [transition]
Species
Homo sapiens
Compartment
ReviewStatus
5/5
Locations in the PathwayBrowser
General
SVG |   | PPTX  | SBGN
Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout
At mitotic entry, EML4 undergoes phosphorylation on serine and/or threonine residues (Pollmann et al. 2006). NEK6 and NEK7 serine/threonine kinases phosphorylate EML4 at evolutionarily conserved serine residues S144 and S146. Phosphorylation of EML4 at S144 and S146 reduces the affinity of EML4 for microtubules, leading to an increase in microtubule instability that is necessary for the assembly of a dynamic mitotic spindle and successful segregation of duplicated chromosomes (Adib et al. 2019).
Literature References
PubMed ID Title Journal Year
31409757 Mitotic phosphorylation by NEK6 and NEK7 reduces the microtubule affinity of EML4 to promote chromosome congression

O'Regan, L, Atherton, J, Straatman, KR, Richards, MW, Bayliss, R, Fry, AM, Straube, A, Moores, CA, Montgomery, JM, Roth, D, Adib, R

Sci Signal 2019
16890222 Human EML4, a novel member of the EMAP family, is essential for microtubule formation

Buck, F, Heidebrecht, HJ, Kruse, ML, Pollmann, M, Parwaresch, R, Adam-Klages, S

Exp. Cell Res. 2006
Participants
Participates
Catalyst Activity

protein serine/threonine kinase activity of p-3S,2T-NEK9: p-S206-NEK6/ p-S195-NEK7 [cytosol]

Orthologous Events
Authored
Reviewed
Created
Cite Us!