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Interplay between Cdh1 and JNK activity during the cell cycle.


ABSTRACT: 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 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.

SUBMITTER: Gutierrez GJ 

PROVIDER: S-EPMC2899685 | biostudies-literature | 2010 Jul

REPOSITORIES: biostudies-literature

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Interplay between Cdh1 and JNK activity during the cell cycle.

Gutierrez Gustavo J GJ   Tsuji Toshiya T   Chen Meifan M   Jiang Wei W   Ronai Ze'ev A ZA  

Nature cell biology 20100627 7


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 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  ...[more]

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