Interactions between Rho GTPases and Rho GDP dissociation inhibitor (Rho-GDI)

The Rho-GDP dissociation inhibitor (Rho-GDI) was used as bait in a two-hybrid screen of a human leucocyte cDNA library. Most of the isolated cDNAs encoded GTPases of the Rho subfamily: RhoA, B, C, Rac1, 2, CDC42 and RhoG. The newly discovered RhoH interacted very poorly with Rho-GDI. Another protein...

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Bibliographic Details
Published in:Biochimie 2001-05, Vol.83 (5), p.409-414
Main Authors: Fauré, Julien, Dagher, Marie-Claire
Format: Article
Language:English
Subjects:
Amino Acid Sequence
beta-Galactosidase
DNA, Complementary
DNA, Complementary - metabolism
Gene Library
Glutathione Transferase
Glutathione Transferase - metabolism
Guanine Nucleotide Dissociation Inhibitors
Guanine Nucleotide Dissociation Inhibitors - chemistry
Guanine Nucleotide Dissociation Inhibitors - metabolism
Humans
Immunology
Innate immunity
Leukocytes
Leukocytes - metabolism
Life Sciences
Lipid Metabolism
Molecular Sequence Data
Mutation
prenylation
Protein Binding
Protein Prenylation
Protein Structure, Tertiary
Recombinant Fusion Proteins
Recombinant Fusion Proteins - metabolism
Rho GDP dissociation inhibitor
rho GTP-Binding Proteins
rho GTP-Binding Proteins - chemistry
rho GTP-Binding Proteins - metabolism
Rho GTPases
rho-Specific Guanine Nucleotide Dissociation Inhibitors
Sequence Homology, Amino Acid
two-hybrid system
Two-Hybrid System Techniques
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Summary:The Rho-GDP dissociation inhibitor (Rho-GDI) was used as bait in a two-hybrid screen of a human leucocyte cDNA library. Most of the isolated cDNAs encoded GTPases of the Rho subfamily: RhoA, B, C, Rac1, 2, CDC42 and RhoG. The newly discovered RhoH interacted very poorly with Rho-GDI. Another protein partner shared a homology with RhoA that points to Asp67 RhoA-Arg68 RhoA-Leu69 RhoA as critical for interaction with Rho-GDI. A second screen with RhoA as bait led to the isolation of GDI only. In order to investigate the relative role of protein-protein and protein-lipid interactions between Rho GTPases and Rho-GDI, CAAX box mutants of RhoA were produced. They were found to interact with Rho-GDI as efficiently as wild type RhoA, indicating that protein-protein interactions alone lead to strong binding of the two proteins. The C-terminal polybasic region of RhoA was also shown to be a site of protein-protein interaction with Rho-GDI.
ISSN:0300-9084
1638-6183
DOI:10.1016/S0300-9084(01)01263-9