Characterization of RAC3, a Novel Member of the Rho Family

The small GTP-binding proteins Rac1 and Rac2 are critically important in regulating multiple signal transduction pathways in eukaryotic cells. Here we report the isolation of a novel third Rac family member, Rac3. Rac3 differs from Rac1/2 at its carboxyl-terminal end, a domain associated with subcel...

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Bibliographic Details
Published in:The Journal of biological chemistry 1997-08, Vol.272 (33), p.20384-20388
Main Authors: Haataja, Leena, Groffen, John, Heisterkamp, Nora
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Base Sequence
Cell Line
Chromosome Mapping
DNA, Complementary - isolation & purification
GTP Phosphohydrolases - metabolism
GTP-Binding Proteins - genetics
GTP-Binding Proteins - isolation & purification
GTP-Binding Proteins - physiology
Humans
Molecular Sequence Data
rac GTP-Binding Proteins
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Summary:The small GTP-binding proteins Rac1 and Rac2 are critically important in regulating multiple signal transduction pathways in eukaryotic cells. Here we report the isolation of a novel third Rac family member, Rac3. Rac3 differs from Rac1/2 at its carboxyl-terminal end, a domain associated with subcellular localization and binding to specific cellular regulators.RAC3 mRNA expression patterns differ from those ofRAC2, which is hematopoietic specific and also from those of RAC1. The RAC3 gene was mapped to chromosome 17q23–25, a region frequently deleted in breast cancer. Rac3 protein levels are not affected by organization of the actin cytoskeleton but remarkably, are serum-inducible. Rac3 is an active GTPase, and this activity is regulated by Bcr. When constitutively activated, Rac3 is able to stimulate efficiently the c-Jun amino-terminal kinase signaling pathway. These findings support a role for Rac3 in intracellular signaling.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.272.33.20384