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Published online 21 February 2006. doi:10.1083/jcb.200508154
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 172, Number 5, 679-692
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Article

 Repo-Man recruits PP1{gamma} to chromatin and is essential for cell viability

Laura Trinkle-Mulcahy1, Jens Andersen2, Yun Wah Lam1, Greg Moorhead3, Matthias Mann2, and Angus I. Lamond1

1 University of Dundee, Dundee DD1 5EH, Scotland, UK
2 University of Southern Denmark, Odense Campusvej 55, DS-5230 Odense M, Denmark
3 University of Calgary, Calgary, Alberta, Canada T2N 1N4

Correspondence to Laura Trinkle-Mulcahy: l.trinklemulcahy{at}dundee.ac.uk

Protein phosphatase 1 (PP1) is a ubiquitous serine/threonine phosphatase regulating many cellular processes. PP1{alpha} and -{gamma} are closely related isoforms with distinct localization patterns, shown here by time-lapse microscopy of stably expressed fluorescent protein fusions. A pool of PP1{gamma} 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 PP1{gamma} 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 PP1{alpha} and -{gamma} in vivo. When overexpressed, Repo-Man can also recruit PP1{alpha} 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 PP1{gamma} and is required for the recruitment of PP1 to chromatin.

Abbreviations used in this paper: DIC, differential interference contrast; FP, fluorescent protein; FRET, fluorescent resonance energy transfer; PP1, protein phosphatase 1; RNAi, RNA interference; siRNA, small interfering RNA; SILAC, stable isotope labeling of amino acids in cell culture.


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