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Elife 2016 Nov 01;5. doi: 10.7554/eLife.19298.
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CPEB4 is regulated during cell cycle by ERK2/Cdk1-mediated phosphorylation and its assembly into liquid-like droplets.

Guillén-Boixet J , Buzon V , Salvatella X , Méndez R .

The four members of the vertebrate CPEB family of RNA-binding proteins share similar RNA-binding domains by which they regulate the translation of CPE-containing mRNAs, thereby controlling cell cycle and differentiation or synaptic plasticity. However, the N-terminal domains of CPEBs are distinct and contain specific regulatory post-translational modifications that presumably differentially integrate extracellular signals. Here we show that CPEB4 activity is regulated by ERK2- and Cdk1-mediated hyperphosphorylation. These phosphorylation events additively activate CPEB4 in M-phase by maintaining it in its monomeric state. In contrast, unphosphorylated CPEB4 phase separates into inactive, liquid-like droplets through its intrinsically disordered regions in the N-terminal domain. This dynamic and reversible regulation of CPEB4 is coordinated with that of CPEB1 through Cdk1, which inactivates CPEB1 while activating CPEB4, thereby integrating phase-specific signal transduction pathways to regulate cell cycle progression.

PubMed ID: 27802129
PMC ID: PMC5089860
Article link: Elife
Grant support: [+]

Species referenced: Xenopus
Genes referenced: aurka cdc20 cdk1 cpeb1 cpeb2 cpeb3 cpeb4 cpsf2 ddx6 fbxo43 isyna1 mapk1 mnt mtor parn plk1 spop tent2
Antibodies: Cdk1 Ab1 Cpeb4 Ab1 Mapk1 Ab10 Papd4 Ab2

Article Images: [+] show captions
References [+] :
Afroz, A fly trap mechanism provides sequence-specific RNA recognition by CPEB proteins. 2014, Pubmed