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PP1/Repo-Man Dephosphorylates Mitotic Histone H3 at T3 and Regulates Chromosomal Aurora B Targeting
- Source :
-
Current Biology . May2011, Vol. 21 Issue 9, p766-773. 8p. - Publication Year :
- 2011
-
Abstract
- Summary: The transient mitotic histone H3 phosphorylation by various protein kinases regulates chromosome condensation and segregation, but the counteracting phosphatases have been poorly characterized []. We show here that PP1γ is the major histone H3 phosphatase acting on the mitotically phosphorylated (ph) residues H3T3ph, H3S10ph, H3T11ph, and H3S28ph. In addition, we identify Repo-Man, a chromosome-bound interactor of PP1γ [], as a selective regulator of H3T3ph and H3T11ph dephosphorylation. Repo-Man promotes H3T11ph dephosphorylation by an indirect mechanism but directly and specifically targets H3T3ph for dephosphorylation by associated PP1γ. The PP1γ/Repo-Man complex opposes the protein kinase Haspin-mediated spreading of H3T3ph to the chromosome arms until metaphase and catalyzes the net dephosphorylation of H3T3ph at the end of mitosis. Consistent with these findings, Repo-Man modulates in a PP1-dependent manner the H3T3ph-regulated chromosomal targeting of Aurora kinase B and its substrate MCAK. Our study defines a novel mechanism by which PP1 counteracts Aurora B. [ABSTRACT FROM AUTHOR]
- Subjects :
- *HISTONES
*CHROMOSOMES
*PHOSPHORYLATION
*PROTEIN kinases
*PHOSPHATASES
*ENZYMES
Subjects
Details
- Language :
- English
- ISSN :
- 09609822
- Volume :
- 21
- Issue :
- 9
- Database :
- Academic Search Index
- Journal :
- Current Biology
- Publication Type :
- Academic Journal
- Accession number :
- 60519668
- Full Text :
- https://doi.org/10.1016/j.cub.2011.03.047