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J Biol Chem, Vol. 273, Issue 30, 18943-18949, July 24, 1998
From the Department of Pharmacology, Kyoto University Faculty of
Medicine, Sakyo-ku, Kyoto 606, Japan and the ¶ CRC Oncogene and
Signal Transduction Group, MRC Laboratory for Molecular Cell Biology
and Department of Biochemistry, University College London, Gower
Street, London WC1E 6BT, United Kingdom
Based on their Rho binding motifs several Rho
target molecules can be classified into three groups; class I includes
the protein kinase PKN, rhophilin, and rhotekin, class II includes the
protein kinases, Rho-associated coiled-coil containing protein kinases, ROCK-I and ROCK-II, and class III includes citron. Taking advantage of
the selectivity in recognition by these targets between Rho and Rac, we
examined the regions in Rho required for selective binding of each
class of Rho target molecules. Yeast two-hybrid assays were performed
using Rho/Rac chimeras and either rhophilin, ROCK-I, or citron. This
study showed the existence of at least two distinct regions in Rho
(amino acids 23-40 and 75-92) that are critical for the selective
binding of these targets. The former was required for binding to
citron, whereas the latter was necessary for binding to rhophilin. On
the other hand, either region showed affinity to ROCK-I. This was
further confirmed by ligand overlay assay using both recombinant ROCK-I
and ROCK-II proteins. Consistently, Rho/Rac chimeras containing either
region can induce stress fibers in transfected HeLa cells, and this
induction is suppressed by treatment with Y-27632, a specific inhibitor
of ROCK kinases. These results suggest that the selective binding of
different classes of Rho targets to Rho is determined by interaction
between distinct Rho-binding motifs of the targets and different
regions of Rho.
Different Regions of Rho Determine Rho-selective Binding of
Different Classes of Rho Target Molecules
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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