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J Biol Chem, Vol. 274, Issue 25, 17763-17770, June 18, 1999

Effector Recognition by the Small GTP-binding Proteins Ras and Ral

Bettina BauerDagger , Gladys Mireyparallel , Ingrid R. VetterDagger , Juan A. García-RaneaDagger Dagger , Alfonso ValenciaDagger Dagger , Alfred WittinghoferDagger , Jacques H. Camonisparallel , and Robbert H. CoolDagger

From the Dagger  Max-Planck-Institut für Molekulare Physiologie, Abteilung Strukturelle Biologie, Otto-Hahn-Strasse 11, D-44227 Dortmund, Germany, the parallel  Institut Curie, INSERM 248, 26 rue d'Ulm, F-75248 Paris, Cedex 05, France, and the Dagger Dagger  Protein Design Group, Centro Nationale de Biotecnología, Campus de la Universidad Autónoma, Cantoblanco, Madrid M-28049, Spain

The Ral effector protein RLIP76 (also called RIP/RalBP1) binds to Ral·GTP via a region that shares no sequence homology with the Ras-binding domains of the Ser/Thr kinase c-Raf-1 and the Ral-specific guanine nucleotide exchange factors. Whereas the Ras-binding domains have a similar ubiquitin-like structure, the Ral-binding domain of RLIP was predicted to comprise a coiled-coil region. In order to obtain more information about the specificity and the structural mode of the interaction between Ral and RLIP, we have performed a sequence space and a mutational analysis. The sequence space analysis of a comprehensive nonredundant assembly of Ras-like proteins strongly indicated that positions 36 and 37 in the core of the effector region are tree-determinant positions for all subfamilies of Ras-like proteins and dictate the specificity of the interaction of these GTPases with their effector proteins. Indeed, we could convert the specific interaction with Ras effectors and RLIP by mutating these residues in Ras and Ral. We therefore conclude that positions 36 and 37 are critical for the discrimination between Ras and Ral effectors and that, despite the absence of sequence homology between the Ral-binding and the Ras-binding domains, their mode of interaction is most probably similar.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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