Repo-Man recruits PP1γ to chromatin and is essential for cell viability

Research output: Journal Publications and Reviews (RGC: 21, 22, 62)21_Publication in refereed journalpeer-review

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Author(s)

  • Laura Trinkle-Mulcahy
  • Jens Andersen
  • Greg Moorhead
  • Matthias Mann
  • Angus I. Lamond

Detail(s)

Original languageEnglish
Pages (from-to)679-692
Journal / PublicationJournal of Cell Biology
Volume172
Issue number5
Publication statusPublished - 27 Feb 2006
Externally publishedYes

Abstract

Protein phosphatase 1 (PP1) is a ubiquitous serine/threonine phosphatase regulating many cellular processes. PP1α and -γ are closely related isoforms with distinct localization patterns, shown here by time-lapse microscopy of stably expressed fluorescent protein fusions. A pool of PP1γ is selectively loaded onto chromatin at anaphase. Using stable isotope labeling and proteomics, we identified a novel PP1 binding protein, Repo-Man, which selectively recruits PP1γ onto mitotic chromatin at anaphase and into the following interphase. This approach revealed both novel and known PP1 binding proteins, quantitating their relative distribution between PP1α and -γ in vivo. When overexpressed, Repo-Man can also recruit PP1́ to chromatin. Mutating Repo-Man's PP1 binding domain does not disrupt chromatin binding but abolishes recruitment of PP1 onto chromatin. RNA interference-induced knockdown of Repo-Man caused large-scale cell death by apoptosis, as did overexpression of this dominant-negative mutant. The data indicate that Repo-Man forms an essential complex with PP1γ and is required for the recruitment of PP1 to chromatin. © The Rockefeller University Press.

Citation Format(s)

Repo-Man recruits PP1γ to chromatin and is essential for cell viability. / Trinkle-Mulcahy, Laura; Andersen, Jens; Yun, Wah Lam; Moorhead, Greg; Mann, Matthias; Lamond, Angus I.

In: Journal of Cell Biology, Vol. 172, No. 5, 27.02.2006, p. 679-692.

Research output: Journal Publications and Reviews (RGC: 21, 22, 62)21_Publication in refereed journalpeer-review