Cited by 243Protein Kinase Regulation and GTPase SignalingCellular transport and secretionProtein Tyrosine Phosphatases

Characterization of RAC3, a Novel Member of the Rho Family

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Haataja, Leena, Groffen, John, Heisterkamp, Nora·1997·Journal of Biological Chemistry

Abstract

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 of RAC2, 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.

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Crossref · 10.1074/jbc.272.33.20384

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  • Rac2 is only expressed in hematopoietic and endothelial cells, whereas Rac1 and Rac3 are ubiquitously expressed in mammalian systems.

    “Rac2 is only expressed in hematopoietic and endothelial cells whereas Rac1 and Rac3 are ubiquitously expressed in mammalian systems [3], [4], [5].”

    From Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo (2014) · cites this paper as [4]

    The Results (page unavailable) report RAC1 and RAC3 mRNA in all human cell lines studied and RAC2 mRNA mainly in hematopoietic cell lines. They do not establish ubiquitous RAC1 or RAC3 expression across mammalian systems or the claimed endothelial-cell expression of RAC2; RAC3 was detected in only some of the tissues listed. (LLM, conf=0.88)

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Research works printed but not linked: 1

  1. Cropp, C. S., Lidereau, R., Campbell, G., Champene, M. H., and Callahan, R. (1990) Proc. Natl. Acad. Sci. U. S. A. 87, 7737-7741

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Authors
Haataja, L., Groffen, J., & Heisterkamp, N.
Affiliations
University of Southern California (US)
Corresponding author
Heisterkamp, Nora
Venue
Journal of Biological Chemistry
Publisher
Elsevier BV
Published
1997-08
Volume
272
Issue
33
Pages
20384-20388
ISSN
0021-9258 (ISSN-L)
OpenAlex
W2049405895
Cited by
243
References
1
Citations by year
2026: 2 · 2025: 5 · 2024: 7 · 2023: 2 · 2022: 15 · 2021: 6 · 2020: 5 · 2019: 3 · 2018: 7 · 2017: 7 · 2016: 4 · 2015: 9 · 2014: 8 · 2013: 6 · 2012: 8
FWCI
2.26
Type
journal article
Language
en
Open access
Locations
  • Journal of Biological Chemistry (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • eScholarship (California Digital Library) (submittedVersion)
Funders
  • National Institutes of Health (-0001)
  • National Cancer Institute (CA-47456, CA 50248, R01CA050248)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Keywords
RAC3, Rho GTPases, small GTPases, Rac1, Rac2, gene isolation, mRNA expression patterns, actin cytoskeleton, BCR, JNK signaling, signal transduction
MeSH terms
Amino Acid Sequence, Base Sequence, Cell Line, Chromosome Mapping, Humans, Molecular Sequence Data, DNA, Complementary, GTP-Binding Proteins, GTP Phosphohydrolases, rac GTP-Binding Proteins

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