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Originally published In Press as doi:10.1074/jbc.M206838200 on September 10, 2002

J. Biol. Chem., Vol. 277, Issue 49, 47331-47337, December 6, 2002
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Binding of the Concave Surface of the Sds22 Superhelix to the alpha 4/alpha 5/alpha 6-Triangle of Protein Phosphatase-1*

Hugo CeulemansDagger §, Veerle VulstekeDagger , Marc De Maeyer||, Kelly Tatchell**, Willy StalmansDagger , and Mathieu BollenDagger

From the Dagger  Afdeling Biochemie, Faculteit Geneeskunde, Katholieke Universiteit Leuven, B-3000 Leuven, Belgium, the || Laboratory for Biomolecular Modelling, Faculteit Wetenschappen, Katholieke Universiteit Leuven, B-3000 Leuven, Belgium, and the ** Department of Biochemistry and Molecular Biology, Louisiana State University Health Sciences Center, Shreveport, Louisiana 71130-3932

Functional studies of the protein phosphatase-1 (PP1) regulator Sds22 suggest that it is indirectly and/or 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 chimeric 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 PP1gamma 1. Within this region, a major interaction site was mapped to a triangular region delineated by the alpha 4-, alpha 5-, and alpha 6-helices. Our data also show that well known regulatory binding sites of PP1, such as the RVXF-binding channel, the beta 12/beta 13-loop, and the acidic groove, are not essential for the interaction with Sds22.

* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Postdoctoral fellow of the Fund for Scientific Research-Flanders. To whom correspondence should be addressed: Afdeling Biochemie, Campus Gasthuisberg, Herestraat 49, B-3000 Leuven, Belgium. Tel.: 32-16-34-57-01; Fax: 32-16-34-59-95; E-mail: Hugo.Ceulemans@med.kuleuven.ac.be.

Postdoctoral fellow of the Fund for Scientific Research-Flanders.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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