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PMID:9113980

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Citation

Adra, CN, Manor, D, Ko, JL, Zhu, S, Horiuchi, T, Van Aelst, L, Cerione, RA and Lim, B (1997) RhoGDIgamma: a GDP-dissociation inhibitor for Rho proteins with preferential expression in brain and pancreas. Proc. Natl. Acad. Sci. U.S.A. 94:4279-84

Abstract

GDP-dissociation inhibitors (GDIs) play a primary role in modulating the activation of GTPases and may also be critical for the cellular compartmentalization of GTPases. RhoGDI and GDI/D4 are two currently known GDIs for the Rho-subfamily of GTPases. Using their cDNAs to screen a human brain cDNA library under low stringency, we have cloned a homologous cDNA preferentially expressed at high levels in brain and pancreas. The predicted protein, named RhoGDIgamma, is approximately 50% identical to GDI/D4 and RhoGDI. It binds to CDC42 and RhoA with less affinity compared with RhoGDI and does not bind with Rac1, Rac2, or Ras. RhoGDIgamma functions as a GDI for CDC42 but with approximately 20 times less efficiency than RhoGDI. Immunohistochemical studies showed a diffuse punctate distribution of the protein in the cytoplasm with concentration around the nucleus in cytoplasmic vesicles. Overexpression of the protein in baby hamster kidney cells caused the cells to round up with loss of stress fibers. A distinct hydrophobic amino terminus in RhoGDIgamma, not seen in the other two RhoGDIs, could provide a mechanism for localization of the GDI to specific membranous compartment thus determining function distinct from RhoGDI or GDI/D4. Our results provide evidence that there is a family of GDIs for the Rho-related GTPases and that they differ in binding affinity, target specificity, and tissue expression. We propose that RhoGDI be renamed RhoGDIalpha and GDID4 be renamed RhoGDIbeta. The new GDI should widen the scope of investigation of this important class of regulatory protein.

Links

PubMed PMC20713

Keywords

Amino Acid Sequence; Base Sequence; Brain/metabolism; Cell Compartmentation; Cloning, Molecular; DNA, Complementary/genetics; Fluorescent Antibody Technique; GTP-Binding Proteins/antagonists & inhibitors; GTP-Binding Proteins/genetics; GTP-Binding Proteins/isolation & purification; GTP-Binding Proteins/metabolism; Guanine Nucleotide Dissociation Inhibitors; Guanosine Diphosphate/metabolism; Humans; Molecular Sequence Data; Pancreas/metabolism; Protein Binding; Sequence Analysis, DNA; Sequence Homology, Amino Acid; Tissue Distribution; rho GTP-Binding Proteins; rho Guanine Nucleotide Dissociation Inhibitor gamma

Significance

Annotations

Gene product Qualifier GO Term Evidence Code with/from Aspect Extension Notes Status

HUMAN:GDIR2

located_in

GO:0031410: cytoplasmic vesicle

ECO:0000304: author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

HUMAN:GDIR3

located_in

GO:0031410: cytoplasmic vesicle

ECO:0000304: author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

HUMAN:GDIR3

enables

GO:0005094: Rho GDP-dissociation inhibitor activity

ECO:0000304: author statement supported by traceable reference used in manual assertion

F

Seeded From UniProt

complete

HUMAN:GDIR3

involved_in

GO:0007162: negative regulation of cell adhesion

ECO:0000304: author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

HUMAN:GDIR3

involved_in

GO:0007266: Rho protein signal transduction

ECO:0000304: author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete

HUMAN:GDIR2

part_of

GO:0031410: cytoplasmic vesicle

ECO:0000304: author statement supported by traceable reference used in manual assertion

C

Seeded From UniProt

complete

HUMAN:GDIR2

involved_in

GO:0007162: negative regulation of cell adhesion

ECO:0000304: author statement supported by traceable reference used in manual assertion

P

Seeded From UniProt

complete


See also

References

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