FBXL7 down-regulates AURKA during mitotic entry and in early mitosis

Stable Identifier
Homo sapiens
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The protein levels of aurora kinase A (AURKA) during mitotic entry and in early mitosis can be reduced by the action of the SCF-FBXL7 E3 ubiquitin ligase complex consisting of SKP1, CUL1, RBX1 and FBXL7 subunits. FBXL7 is the substrate recognition subunit of the SCF-FBXL7 complex that associates with the centrosome-bound AURKA, promoting its ubiquitination and proteasome-mediated degradation. Overexpression of FBXL7 results in G2/M cell cycle arrest and apoptosis (Coon et al. 2011).

FBXL7 protein levels are down-regulated by the action of the SCF-FBXL18 E3 ubiquitin ligase complex, consisting of SKP1, CUL1, RBX1 and the substrate recognition subunit FBXL18. FBXL18 binds to the FQ motif of FBXL7, targeting it for ubiquitination and proteasome-mediated degradation, counteracting its pro-apoptotic activity (Liu et al. 2015). Cell cycle stage-dependency of down-regulation of FBXL7 by FBXL18 is unknown.

Literature References
PubMed ID Title Journal Year
25654763 F-box protein Fbxl18 mediates polyubiquitylation and proteasomal degradation of the pro-apoptotic SCF subunit Fbxl7

Zou, C, Liu, Y, Chen, BB, Lear, T, Mallampalli, RK, Zhao, Y, Zhao, J

Cell Death Dis 2015
22306998 Novel E3 ligase component FBXL7 ubiquitinates and degrades Aurora A, causing mitotic arrest

Glasser, JR, Chen, BB, Coon, TA, Mallampalli, RK

Cell Cycle 2012
Event Information
Orthologous Events
Cross References
BioModels Database
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