Developmental Cell
Volume 21, Issue 2, 16 August 2011, Pages 328-342
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Article
Repo-Man Coordinates Chromosomal Reorganization with Nuclear Envelope Reassembly during Mitotic Exit

https://doi.org/10.1016/j.devcel.2011.06.020Get rights and content
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Summary

Repo-Man targets protein phosphatase 1 γ (PP1γ) to chromatin at anaphase onset and regulates chromosome structure during mitotic exit. Here, we show that a Repo-Man:PP1 complex forms in anaphase following dephosphorylation of Repo-Man. Upon activation, the complex localizes to chromosomes and causes the dephosphorylation of histone H3 (Thr3, Ser10, and Ser28). In anaphase, Repo-Man has both catalytic and structural functions that are mediated by two separate domains. A C-terminal domain localizes Repo-Man to bulk chromatin in early anaphase. There, it targets PP1 for the dephosphorylation of histone H3 and possibly other chromosomal substrates. An N-terminal domain localizes Repo-Man to the chromosome periphery later in anaphase. There, it is responsible for the recruitment of nuclear components such as Importin β and Nup153 in a PP1-independent manner. These observations identify Repo-Man as a key factor that coordinates chromatin remodeling and early events of nuclear envelope reformation during mitotic exit.

Highlights

► Repo-Man/PP1 complex is activated in anaphase by Repo-Man dephosphorylation ► Repo-Man/PP1 dephosphorylates histone H3 at Thr3, Ser10, and Ser28 ► Repo-Man binds Importin β in anaphase and targets it to the chromosome periphery ► Repo-Man has both catalytic and structural functions during mitotic exit

Cited by (0)

3

Present address: Department of Cellular and Molecular Pharmacology, University of California, San Francisco, San Francisco, CA 94158-2517, USA

4

Present address: Department of Molecular Cell Biology, University of Leuven, B-3000 Leuven, Belgium