1. Repo-Man coordinates chromosomal reorganization with nuclear envelope reassembly during mitotic exit.
- Author
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Vagnarelli P, Ribeiro S, Sennels L, Sanchez-Pulido L, de Lima Alves F, Verheyen T, Kelly DA, Ponting CP, Rappsilber J, and Earnshaw WC
- Subjects
- Anaphase genetics, Anaphase physiology, Carrier Proteins genetics, Cell Cycle Proteins genetics, Cell Line, Transformed, Cyclin B metabolism, Gene Expression Regulation physiology, Green Fluorescent Proteins genetics, Histones metabolism, Humans, Mitosis genetics, Models, Biological, Nuclear Proteins genetics, Phosphorylation physiology, Protein Binding genetics, Protein Structure, Tertiary physiology, RNA Interference physiology, Receptors, Neuropeptide Y genetics, Receptors, Neuropeptide Y metabolism, Tandem Mass Spectrometry methods, Transfection, beta Karyopherins metabolism, Carrier Proteins metabolism, Cell Cycle Proteins metabolism, Chromosomes metabolism, Mitosis physiology, Nuclear Envelope physiology, Nuclear Proteins metabolism
- Abstract
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., (Copyright © 2011 Elsevier Inc. All rights reserved.)
- Published
- 2011
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