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Title: Docking motif-guided mapping of the interactome of protein phosphatase-1
Authors: Hendrickx, Annick *
Beullens, Monique *
Ceulemans, Hugo *
Den Abt, Tom
Van Eynde, Aleyde
Nicolaescu, Emilia
Lesage, Bart
Bollen, Mathieu # ×
Issue Date: Apr-2009
Publisher: Current Biology Ltd.
Series Title: Chemistry & Biology vol:16 issue:4 pages:365-71
Abstract: The ubiquitous protein Ser/Thr phosphatase-1 (PP1) interacts with dozens of regulatory proteins that are structurally unrelated. However, most of them share a short, degenerate "RVxF"-type docking motif. Using a broad in silico screening based on a stringent definition of the RVxF motif, in combination with a multistep biochemical validation procedure, we have identified 78 novel mammalian PP1 interactors. A global analysis of the validated RVxF-based PP1 interactome not only provided insights into the conserved features of the RVxF motif but also led to the discovery of additional common PP1 binding elements, described as the "SILK" and "MyPhoNE" motifs. In addition to the doubling of the known mammalian PP1 interactome, our data contribute to the design of PP1 interaction networks. Notably, an interaction network linking PP1 interactors discloses a pleiotropic role of PP1 in cell polarity.
URI: 
ISSN: 1074-5521
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Microbiology and Biotechnology Section - miscellaneous
Laboratory of Biosignaling & Therapeutics
* (joint) first author
× corresponding author
# (joint) last author

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