Cited by 164Protein Kinase Regulation and GTPase SignalingCellular transport and secretionProtein Tyrosine Phosphatases

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Identification of Guanine Nucleotide Exchange Factors (GEFs) for the Rap1 GTPase

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Rebhun, John F., Castro, Ariel F., Quilliam, Lawrence A.·2000·Journal of Biological Chemistry

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Abstract

Although the Ras subfamily of GTPases consists of approximately 20 members, only a limited number of guanine nucleotide exchange factors (GEFs) that couple extracellular stimuli to Ras protein activation have been identified. Furthermore, no novel downstream effectors have been identified for the M-Ras/R-Ras3 GTPase. Here we report the identification and characterization of three Ras family GEFs that are most abundantly expressed in brain. Two of these GEFs, MR-GEF (M-Ras-regulated GEF, KIAA0277) and PDZ-GEF (KIAA0313) bound specifically to nucleotide-free Rap1 and Rap1/Rap2, respectively. Both proteins functioned as Rap1 GEFs in vivo. A third GEF, GRP3 (KIAA0846), activated both Ras and Rap1 and shared significant sequence homology with the calcium- and diacylglycerol-activated GEFs, GRP1 and GRP2. Similarly to previously identified Rap GEFs, C3G and Smg GDS, each of the newly identified exchange factors promoted the activation of Elk-1 in the LNCaP prostate tumor cell line where B-Raf can couple Rap1 to the extracellular receptor-activated kinase cascade. MR-GEF and PDZ-GEF both contain a region immediately N-terminal to their catalytic domains that share sequence homology with Ras-associating or RalGDS/AF6 homology (RA) domains. By searching for in vitro interaction with Ras-GTP proteins, PDZ-GEF specifically bound to Rap1A- and Rap2B-GTP, whereas MR-GEF bound to M-Ras-GTP. C-terminally truncated MR-GEF, lacking the GEF catalytic domain, retained its ability to bind M-Ras-GTP, suggesting that the RA domain is important for this interaction. Co-immunoprecipitation studies confirmed the interaction of M-Ras-GTP with MR-GEF in vivo. In addition, a constitutively active M-Ras(71L) mutant inhibited the ability of MR-GEF to promote Rap1A activation in a dose-dependent manner. These data suggest that M-Ras may inhibit Rap1 in order to elicit its biological effects.

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Authors: Rebhun, J. F., Castro, A. F., & Quilliam, L. A.
Affiliations: Indiana University Indianapolis (US)
Corresponding author: Quilliam, Lawrence A.
ORCID: Rebhun, John F.
Castro, Ariel F.
Venue: Journal of Biological Chemistry
Publisher: Elsevier BV
Published: 2000-11
Volume: 275
Issue: 45
Pages: 34901-34908
ISSN: 0021-9258 (ISSN-L)
DOI: 10.1074/jbc.m005327200
OpenAlex: W2033334272
Cited by: 164
References: 56
Citations by year: 2026: 4 · 2025: 5 · 2024: 3 · 2023: 3 · 2022: 3 · 2021: 2 · 2020: 3 · 2019: 8 · 2018: 7 · 2017: 4 · 2016: 7 · 2015: 2 · 2014: 6 · 2013: 3 · 2012: 13
FWCI: 3.49
Type: journal article
Language: en
Open access: hybrid
doi.org
Licence: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 7275 d)
Locations: Journal of Biological Chemistry (publishedVersion, cc-by)
PubMed (publishedVersion)
Funders: National Cancer Institute
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: guanine nucleotide exchange factor, Rap1 GTPase, M-Ras, Ras family GTPases, Rap1A, Rap2B, Elk-1, BRAF, GTPase activation, brain
MeSH terms: Amino Acid Sequence, Brain, Calcium, Cell Line, Diglycerides, DNA-Binding Proteins, Dose-Response Relationship, Drug, Enzyme Activation, Humans, Molecular Sequence Data, Nerve Tissue Proteins, Plasmids, Precipitin Tests, Protein Binding, Proto-Oncogene Proteins, Tissue Distribution, Transcription Factors, Tumor Cells, Cultured, Blotting, Northern, Mutagenesis, Sequence Homology, Amino Acid, Protein Structure, Tertiary, DNA, Complementary, Receptors, Cytoplasmic and Nuclear, Proto-Oncogene Proteins c-raf, Catalytic Domain, Guanine Nucleotide Exchange Factors, ras Guanine Nucleotide Exchange Factors, rap GTP-Binding Proteins, rap1 GTP-Binding Proteins, ets-Domain Protein Elk-1

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Identification of Guanine Nucleotide Exchange Factors (GEFs) for the Rap1 GTPase

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