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Cited by 54Protein Kinase Regulation and GTPase SignalingProtein Tyrosine PhosphatasesCellular transport and secretion

The DOI matches its Crossref record; 49 of the 49 references it cites were found in a registry or an index.

M-Ras, a Widely Expressed 29-kD Homologue of p21 Ras: Expression of a Constitutively Active Mutant Results in Factor-Independent Growth of an Interleukin-3–Dependent Cell Line

Ehrhardt, Götz R.A., Leslie, Kevin B., Lee, Frances, Wieler, James S., Schrader, John W.·1999·Blood
DOI 10.1182/blood.v94.7.2433.419k31_2433_2444
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Abstract

M-Ras, a recently identified homologue of p21 Ras, is widely expressed, with levels of the 29-kD protein in spleen, thymus, and NIH 3T3 fibroblasts equaling or exceeding those of p21 Ras. A G22V mutant of M-Ras was constitutively active and its expression in an interleukin-3 (IL-3)–dependent mast cell/megakaryocyte cell line resulted in increased survival in the absence of IL-3, increased growth in IL-4, and, at high expression levels, in factor-independent growth. Expression of M-Ras G22V, however, had a negative effect on growth in the presence of IL-3, suggesting that M-Ras has both positive and negative effects on growth. Expression of M-Ras G22V in NIH-3T3 fibroblasts resulted in morphological transformation and growth to higher cell densities. M-Ras G22V induced activation of thec-fos promoter, and bound weakly to the Ras-binding domains of Raf-1 and RalGDS. Expression of a mutant of M-Ras G22V that was no longer membrane-bound partially inhibited (40%) activation of thec-fos promoter by N-Ras Q61K, suggesting that M-Ras shared some, but not all, of the effectors of N-Ras. An S27N mutant of M-Ras, like the analogous H-Ras S17N mutant, was a dominant inhibitor of activation of the c-fos promoter by constitutively active Src Y527F, suggesting that M-Ras and p21 Ras shared guanine nucleotide exchange factors and are likely to be activated in parallel. Moreover, M-Ras was recognized by the monoclonal anti-Ras antibody Y13-259, commonly used to study the function and activity of p21 Ras. Mammalian M-Ras and a Caenorhabditis elegans orthologue exhibit conserved structural features, and these are likely to mediate activation of distinctive signaling paths that function in parallel to those downstream of p21 Ras.

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Crossref · 10.1182/blood.v94.7.2433.419k31_2433_2444

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Metadata

Authors
Ehrhardt, G. R. A., Leslie, K. B., Lee, F., Wieler, J. S., & Schrader, J. W.
Affiliations
  • From The Biomedical Research Centre, University of British Columbia, Vancouver, BC, Canada.
  • University of British Columbia (CA)
ORCID
Schrader, John W.
Venue
Blood
Publisher
American Society of Hematology
Published
1999-10-01
Volume
94
Issue
7
Pages
2433-2444
ISSN
  • 0006-4971 (ISSN-L)
  • 1528-0020
DOI
10.1182/blood.v94.7.2433.419k31_2433_2444
OpenAlex
W345372262
Cited by
54
References
49
Citations by year
2026: 1 · 2025: 1 · 2024: 2 · 2022: 1 · 2019: 1 · 2018: 3 · 2017: 2 · 2016: 1 · 2015: 3 · 2013: 2
FWCI
1.61
Type
journal article
Language
en
Open access
closed
Locations
  • Blood (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords
M-Ras, interleukin-3 dependence, guanine nucleotide exchange factor, Raf-1, RalGDS, Src kinase, NIH3T3 cells, morphological transformation, Ras signaling
MeSH terms
Amino Acid Sequence, Animals, Antibodies, Epitopes, Cell Division, Cell Line, Cell Line, Transformed, Humans, Interleukin-3, Molecular Sequence Data, Molecular Weight, Recombinant Proteins, Tumor Cells, Cultured, Proto-Oncogene Proteins p21(ras), Mutagenesis, Site-Directed, Sequence Alignment, 3T3 Cells, Culture Media, Conditioned, ras Proteins, Amino Acid Substitution, Monomeric GTP-Binding Proteins, Mice

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