Author: ["Gustavo J. Gutierrez","Toshiya Tsuji","Meifan Chen","Wei Jiang","Ze'ev A. Ronai"]
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Abstract
The stress-activated kinase, JNK, is regulated by the anaphase promoting complex (APC) ubiquitin ligase. Conversely, JNK also negatively controls the APC by directly phosphorylating the Cdh1 component of the APC and decreasing its affinity for the APC core subunits. The ubiquitin ligase APC/CCdh1 coordinates degradation of key cell cycle regulators. We report here that a nuclear-localized portion of the stress-activated kinase JNK is degraded by the APC/CCdh1 during exit from mitosis and the G1 phase of the cell cycle. Expression of a non-degradable JNK induces prometaphase-like arrest and aberrant mitotic spindle dynamics. Moreover, JNK phosphorylates Cdh1 directly, during G2 and early mitosis, changing its subcellular localization and attenuating its ability to activate the APC/C during G2/M. This regulatory mechanism between JNK and Cdh1 reveals an important function for JNK during the cell cycle.Cite this article
Gutierrez, G., Tsuji, T., Chen, M. et al. Interplay between Cdh1 and JNK activity during the cell cycle. Nat Cell Biol 12, 686–695 (2010). https://doi.org/10.1038/ncb2071 