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Papers In Press, published online ahead of print September 10, 2002
J. Biol. Chem, 10.1074/jbc.M206838200
Submitted on July 9, 2002
Revised on September 9, 2002
Accepted on September 10, 2002

Binding of the concave surface of the Sds22 superhelix to the alpha4/alpha5/alpha6-triangle of protein phosphatase-1

Hugo Ceulemans, Veerle Vulsteke, Marc De Maeyer, Kelly Tatchell, Willy Stalmans, and Mathieu Bollen

Afdeling Biochemie, KULeuven, Leuven B-3000

Corresponding Author: Mathieu.Bollen{at}med.kuleuven.ac.be

Functional studies of the protein phosphatase-1 (PP1) regulator Sds22 suggest that it is (in)directly involved in one of the most ancient functions of PP1, i.e. reversing phosphorylation by the Aurora-related protein kinases. We predict that the conserved portion of Sds22 folds into a curved superhelix and demonstrate that mutation to alanine of any of eight residues (Asp148, Phe170, Glu192, Phe214, Asp280, Glu300, Trp302 or Tyr327) at the concave surface of this superhelix thwarts the interaction with PP1. Furthermore, we show that all mammalian isoforms of PP1 have the potential to bind Sds22. Interaction studies with truncated versions of PP1 and with chimaeric proteins comprising fragments of PP1 and the yeast PP1-like protein phosphatase Ppz1 suggest that the site(s) required for the binding of Sds22 reside between residues 43 and 173 of PP1gamma1. Within this region, a major interaction site was mapped to a triangular region delineated by the alpha4, alpha5 and alpha6 helices. Our data also show that well-known regulatory binding sites of PP1, such as the RVxF-binding channel, the beta12/beta13-loop and the acidic groove, are not essential for the interaction with Sds22.


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