Phosphorylation of N ‐terminal regions of REV‐ERBs regulates their intracellular localization

In this study, we found that the highly homologous N‐terminal regions of REV‐ERBα and REV‐ERBβ determined both their own CK1‐catalyzed phosphorylation and the cytoplasmic accumulation of each hyperphosphorylated form. Of the homologous N‐terminal regions, three serine‐rich clusters in REV‐ERBβ are required for the phosphorylation and cytoplasmic localization. Our results indicate that the REV‐ERBs phosphorylation by CK1 plays a key role in their subcellular localization, thereby controlling the timings of the transcriptional activation and inhibition of Bmal1.

We found that the highly homologous N‐terminal regions of REV‐ERBα and REV‐ERBβ determined both their own CK1‐catalyzed phosphorylation and the cytoplasmic accumulation of each hyperphosphorylated form. Of the homologous N‐terminal regions, three serine‐rich clusters in REV‐ERBβ are required for the phosphorylation and cytoplasmic localization. Our results indicate that the REV‐ERBs phosphorylation by CK1 plays a key role in their subcellular localization, thereby controlling the timings of the transcriptional activation and inhibition of Bmal1.

Source: Genes to Cells - February 1, 2018 Category: Genetics & Stem Cells Authors: Yuki Ohba, Hajime Tei Tags: ORIGINAL ARTICLE Source Type: research