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Interplay between Cdh1 and JNK activity during the cell cycle

The ubiquitin ligase APC/C(Cdh1) 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/C(Cdh1) during exit from mitosis and G1 phase of the cell cycle. Expression of a non-degradable JNK induces...

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Detalles Bibliográficos
Autores principales: Gutierrez, Gustavo J., Tsuji, Toshiya, Chen, Meifan, Jiang, Wei, Ronai, Ze’ev A.
Formato: Texto
Lenguaje:English
Publicado: 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2899685/
https://www.ncbi.nlm.nih.gov/pubmed/20581839
http://dx.doi.org/10.1038/ncb2071
Descripción
Sumario:The ubiquitin ligase APC/C(Cdh1) 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/C(Cdh1) during exit from mitosis and G1 phase of the cell cycle. Expression of a non-degradable JNK induces prometaphase-like arrest and aberrant mitotic spindle dynamics. Moreover, JNK directly phosphorylates Cdh1, during G2 and early mitosis, changing its subcellular localization and attenuating its ability to activate the APC/C during G2/M. The newly identified regulatory mechanism between JNK and Cdh1 reveals an important function for JNK during the cell cycle.