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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.

Original publication




Journal article


Dev Cell

Publication Date





328 - 342


Anaphase, Carrier Proteins, Cell Cycle Proteins, Cell Line, Transformed, Chromosomes, Cyclin B, Gene Expression Regulation, Green Fluorescent Proteins, Histones, Humans, Mitosis, Models, Biological, Nuclear Envelope, Nuclear Proteins, Phosphorylation, Protein Binding, Protein Structure, Tertiary, RNA Interference, Receptors, Neuropeptide Y, Tandem Mass Spectrometry, Transfection, beta Karyopherins