rac, a novel ras-related family of proteins that are botulinum toxin substrates
Open accessAbstract
A new family of ras-related proteins, designated rac (ras-related C3 botulinum toxin substrate) has been identified. rac1 and rac2 cDNA clones were isolated from a differentiated HL-60 library and encode proteins that are 92% homologous and share 58% and 26-30% amino acid homology with human rhos and ras, respectively. Nucleotide sequence analysis predicts both rac1 and rac2 proteins to contain 192 amino acids with molecular masses of 21,450 and 21,429 daltons, respectively. rac1 and rac2 possess four of the five conserved functional domains in ras associated with binding and hydrolysis of guanine nucleotides. They also contain the COOH-terminal consensus sequence Cys-X-X-X-COOH which localizes ras to the inner plasma membrane and the residues Gly12 and Ala59, at which sites mutations elicit transforming potential to ras. The rac transcripts, particularly rac2, display relative myeloid tissue selectivity. Both rac1 transcripts (2.4 and 1.1 kilobases (kb] increase when HL-60 cells differentiate to neutrophil-like morphology. In contrast, differentiation of U937 cells to monocyte-like morphology causes no change in the 2.4-kb mRNA and a decrease in the 1.1-kb mRNA species. rac2 mRNA (1.45 kb) increases 7-9-fold and 3-fold upon differentiation of HL-60 and U937 cells, respectively. Neither rac mRNAs are present in a Jurkat T cell line, and unlike rac1, rac2 mRNA is absent in human brain and liver tissue. Transfection experiments permitted the demonstration that rac1 and rac2 are…
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Divergent amino acid residues in the β2-β3 regions of Rac and Cdc42 are the major determinants of specific interactions with DH-domain containing GEFs.
“These structural studies have also revealed that divergent amino acid residues in the 2-3 regions of Rac and Cdc42 are the major determinants of specific interactions with DH-domain containing GEFs (26 -29).”
From Specific Recognition of Rac2 and Cdc42 by DOCK2 and DOCK9 Guanine Nucleotide Exchange Factors (2008) · cites this paper as [27]
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 [3]
Among mammalian Rho GTPases, only Rac2 and RhoH are specifically expressed in haematopoietic cells.
“Only two members of the Rho family, Rac2 and RhoH, are specifically expressed in haematopoietic cells [13,14].”
From The small GTPase RhoH is an atypical regulator of haematopoietic cells (2008) · cites this paper as [14]
Cites
Bar-Sagi, D., & Feramisco, J. R. (1986) · Science · doi:10.1126/science.3090687 · Cited by 734 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
The GTPase superfamily: conserved structure and molecular mechanism
Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392 · see citing works
Localization of low molecular weight GTP binding proteins to exocytic and endocytic compartments
Chavrier, P., Parton, R. G., Hauri, H. P., Simons, K., & Zerial, M. (1990) · Cell · doi:10.1016/0092-8674(90)90369-p · Cited by 1,166 · see citing works
Roberts, A. W., Kim, C., Zhen, L., Lowe, J. B., Kapur, R., Petryniak, B., Spaetti, A., Pollock, J. D., Borneo, J. B., Bradford, G. B., et al. (1999) · Immunity · doi:10.1016/s1074-7613(00)80019-9 · Cited by 556 · see citing works
RHO GTPases: from new partners to complex immune syndromes
El Masri, R., & Delon, J. (2021) · Nature Reviews Immunology · doi:10.1038/s41577-021-00500-7 · Cited by 131 · see citing works
Rac2 Controls Tumor Growth, Metastasis and M1-M2 Macrophage Differentiation In Vivo
Joshi, S., Singh, A. R., Zulcic, M., Bao, L., Messer, K., Ideker, T., Dutkowski, J., & Durden, D. L. (2014) · PLoS ONE · doi:10.1371/journal.pone.0095893 · Cited by 128 · see citing works
Isozyme-specific stimulation of phospholipase C-γ2 by Rac GTPases
Piechulek, T., Rehlen, T., Walliser, C., Vatter, P., Moepps, B., & Gierschik, P. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m509396200 · Cited by 80 · see citing works
Rac2 Specificity in Macrophage Integrin Signaling
Pradip, D., Peng, X., & Durden, D. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306491200 · Cited by 49 · see citing works
The small GTPase RhoH is an atypical regulator of haematopoietic cells
Fueller, F., & Kubatzky, K. F. (2008) · Cell Communication and Signaling · doi:10.1186/1478-811x-6-6 · Cited by 40 · see citing works
Specific Recognition of Rac2 and Cdc42 by DOCK2 and DOCK9 Guanine Nucleotide Exchange Factors
Kwofie, M. A., & Skowronski, J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m705170200 · Cited by 36 · see citing works
Bioinformatics analysis of microarray data to reveal the pathogenesis of brain ischemia
He, J., Gao, Y., Wu, G., Lei, X., Zhang, Y., Pan, W., & Yu, H. (2018) · Molecular Medicine Reports · doi:10.3892/mmr.2018.9000 · Cited by 11 · see citing works
- Authors
- Didsbury, J., Weber, R. F., Bokoch, G. M., Evans, T., & Snyderman, R.
- Affiliations
- Genentech (US)
- Scripps Clinic (US)
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1989-10
- Volume
- 264
- Issue
- 28
- Pages
- 16378-16382
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1568345151
- Cited by
- 575
- References
- 1
- Citations by year
- 2026: 3 · 2025: 5 · 2024: 7 · 2023: 21 · 2022: 6 · 2021: 13 · 2020: 9 · 2019: 14 · 2018: 13 · 2017: 13 · 2016: 6 · 2015: 12 · 2014: 12 · 2013: 17 · 2012: 11
- FWCI
- 13.80
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01de003738-25)
- National Institute of General Medical Sciences (GM39434)
- National Institute of Dental and Craniofacial Research (5R01-DE-03738-16)
- 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
- Ras-related proteins, ADP-ribosylation, G proteins, myeloid differentiation, HL-60 cells, U937 cells, plasma membrane localization, secretory regulation
- MeSH terms
- Amino Acid Sequence, Base Sequence, Botulinum Toxins, Cell Line, Cloning, Molecular, DNA, Neoplasm, Humans, Molecular Sequence Data, Proteins, Proto-Oncogene Proteins, Genes, ras, Sequence Homology, Nucleic Acid, Substrate Specificity, Oligonucleotide Probes, Leukemia, Promyelocytic, Acute, Proto-Oncogene Proteins p21(ras), rac GTP-Binding Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
