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

Rebhun, John F.; Castro, Ariel F.; Quilliam, Lawrence A.

doi:10.1074/jbc.m005327200

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

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

DOI 10.1074/jbc.m005327200

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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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MRAS uniquely associates with SHOC2 and PPI1C as well as certain RapGEFs.
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Rap1 controls cell adhesion and cell motility through the regulation of myosin II
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Multiple roles of Rap1 in hematopoietic cells: complementary versus antagonistic functions
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Functional coordination of alternative splicing in the mammalian central nervous system
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The Rac1 C-terminal Polybasic Region Regulates the Nuclear Localization and Protein Degradation of Rac1
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Activity-Dependent Dendritic Spine Structural Plasticity Is Regulated by Small GTPase Rap1 and Its Target AF-6
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Two subclasses of lung squamous cell carcinoma with different gene expression profiles and prognosis identified by hierarchical clustering and non-negative matrix factorization
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Identification and Characterization of RA-GEF-2, a Rap Guanine Nucleotide Exchange Factor That Serves as a Downstream Target of M-Ras
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Cyclic AMP Inhibits Extracellular Signal-regulated Kinase and Phosphatidylinositol 3-Kinase/Akt Pathways by Inhibiting Rap1
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Phorbol esters modulate the Ras exchange factor RasGRP3.
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GNA11 Q209L Mouse Model Reveals RasGRP3 as an Essential Signaling Node in Uveal Melanoma
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Wiskott-Aldrich Syndrome Protein Is a Key Regulator of the Phagocytic Cup Formation in Macrophages
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Functional Implications of miR-19 in the Migration of Newborn Neurons in the Adult Brain
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Somatic gene copy number alterations in colorectal cancer: new quest for cancer drivers and biomarkers
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FBP17 Mediates a Common Molecular Step in the Formation of Podosomes and Phagocytic Cups in Macrophages
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Co-targeting SOS1 enhances the antitumor effects of KRASG12C inhibitors by addressing intrinsic and acquired resistance
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Splice Variants of SmgGDS Control Small GTPase Prenylation and Membrane Localization
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Crystal Structure of M-Ras Reveals a GTP-bound “Off” State Conformation of Ras Family Small GTPases
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Requirement for a Complex of Wiskott-Aldrich Syndrome Protein (WASP) with WASP Interacting Protein in Podosome Formation in Macrophages
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Anthrax Edema Toxin Inhibits Endothelial Cell Chemotaxis via Epac and Rap1
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PKC-θ selectively controls the adhesion-stimulating molecule Rap1
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RA-GEF-1, a Guanine Nucleotide Exchange Factor for Rap1, Is Activated by Translocation Induced by Association with Rap1·GTP and Enhances Rap1-dependent B-Raf Activation
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A multi-ethnic meta-analysis identifies novel genes, including ACSL5, associated with amyotrophic lateral sclerosis
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The PDZ-GEF Dizzy regulates cell shape of migrating macrophages via Rap1 and integrins in theDrosophilaembryo
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The M-Ras-RA-GEF-2-Rap1 Pathway Mediates Tumor Necrosis Factor-α–dependent Regulation of Integrin Activation in Splenocytes
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SmgGDS Regulates Cell Proliferation, Migration, and NF-κB Transcriptional Activity in Non-small Cell Lung Carcinoma
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Deconstructing signal transduction pathways that regulate the actin cytoskeleton in dendritic spines
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Identification of mNET1 as a Candidate Ligand for the First PDZ Domain of MAGI-1
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A Vascular Gene Trap Screen Defines RasGRP3 as an Angiogenesis-Regulated Gene Required for the Endothelial Response to Phorbol Esters
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Discovery and Characterization of Novel Vascular and Hematopoietic Genes Downstream of Etsrp in Zebrafish
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Hepatoma Cells From Mice Deficient in Glycine N-Methyltransferase Have Increased RAS Signaling and Activation of Liver Kinase B1
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Diacylglycerols Containing Omega 3 and Omega 6 Fatty Acids Bind to RasGRP and Modulate MAP Kinase Activation
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E‐cadherin dis‐engagement activates the Rap1 GTPase
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Structural fingerprints, interactions, and signaling networks of RAS family proteins beyond RAS isoforms
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Protein Kinase A-independent Ras Protein Activation Cooperates with Rap1 Protein to Mediate Activation of the Extracellular Signal-regulated Kinases (ERK) by cAMP
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Expression of activated M-Ras in a murine mammary epithelial cell line induces epithelial–mesenchymal transition and tumorigenesis
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Drosophila PDZ-GEF, a Guanine Nucleotide Exchange Factor for Rap1 GTPase, Reveals a Novel Upstream Regulatory Mechanism in the Mitogen-Activated Protein Kinase Signaling Pathway
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M-Ras is activated by bone morphogenetic protein-2 and participates in osteoblastic determination, differentiation, and transdifferentiation
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M-Ras/Shoc2 signaling modulates E-cadherin turnover and cell–cell adhesion during collective cell migration
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Critical Function of the Ras-associating Domain as a Primary Ras-binding Site for Regulation of Saccharomyces cerevisiaeAdenylyl Cyclase
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Genomic differences between estrogen receptor (ER)‐positive and ER‐negative human breast carcinoma identified by single nucleotide polymorphism array comparative genome hybridization analysis
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An online version of the Mooney Face Test: phenotypic and genetic associations
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NCS-Rapgef2, the Protein Product of the NeuronalRapgef2Gene, Is a Specific Activator of D1 Dopamine Receptor-Dependent ERK Phosphorylation in Mouse Brain
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Targeting of nucleotide-binding proteins by HAMLET—a conserved tumor cell death mechanism
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Stromal inhibition of megakaryocytic differentiation is associated with blockade of sustained Rap1 activation
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The RASputin effect: Figure 1.Preprint
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Analysis of Gene Expression Variance in Schizophrenia Using Structural Equation Modeling
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Activation and Function of the Rap1 Gtpase in B Lymphocytes
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Genome-wide expression changes in a higher state of consciousness
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Identification of chromosomal copy number variations and novel candidate loci in hereditary nonpolyposis colorectal cancer with mismatch repair proficiency
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The Exchange Factor and Diacylglycerol Receptor RasGRP3 Interacts with Dynein Light Chain 1 through Its C-terminal Domain
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M‐Ras induces Ral and JNK activation to regulate MEK/ERK‐independent gene expression in MCF‐7 breast cancer cells
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Novel estrogen-responsive genes (ERGs) for the evaluation of estrogenic activity
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Alterations in pectoralis muscle cell characteristics after radiation of the human breast in situ
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Mast Cells in Airway Hyporesponsive C3H/HeJ Mice Express a Unique Isoform of the Signaling Protein Ras Guanine Nucleotide Releasing Protein 4 That Is Unresponsive to Diacylglycerol and Phorbol Esters
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Expression of a constitutively active mutant of M-Ras in normal bone marrow is sufficient for induction of a malignant mastocytosis/mast cell leukemia, distinct from the histiocytosis/monocytic leukemia induced by expression of activated H-Ras
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A genetic factor associated with low final bone mineral density in children after a long-term glucocorticoids treatment
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M-Ras evolved independently of R-Ras and its neural function is conserved between mammalian and ascidian, which lacks classical Ras
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Three‐generation family with novel contiguous gene deletion on chromosome 2p22 associated with thoracic aortic aneurysm syndrome
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MiR-486-5p-directed MAGI1/Rap1/RASSF5 signaling pathway contributes to hydroquinone-induced inhibition of erythroid differentiation in K562 cells
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Genetics of PlGF plasma levels highlights a role of its receptors and supports the link between angiogenesis and immunity
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Identification and Characterization of RA-GEF-2, a Rap Guanine Nucleotide Exchange Factor That Serves as a Downstream Target of M-Ras
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A growing family of guanine nucleotide exchange factors is responsible for activation of ras-family GTPases
Quilliam, L. A., Rebhun, J. F., & Castro, A. F. (2002) · Progress in nucleic acid research and molecular biology · doi:10.1016/s0079-6603(02)71047-7 · Cited by 276 · see citing works
Self-citation
RA-GEF, a Novel Rap1A Guanine Nucleotide Exchange Factor Containing a Ras/Rap1A-associating Domain, Is Conserved between Nematode and Humans
Liao, Y., Kariya, K., Hu, C., Shibatohge, M., Goshima, M., Okada, T., Watari, Y., Gao, X., Jin, T. J., Yamawaki‐Kataoka, Y., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.53.37815 · Cited by 87 · see citing works
RasGEF1A and RasGEF1B are guanine nucleotide exchange factors that discriminate between Rap GTP‐binding proteins and mediate Rap2‐specific nucleotide exchange
Yaman, E., Gasper, R., Koerner, C., Wittinghofer, A., & Tazebay, U. H. (2009) · FEBS Journal · doi:10.1111/j.1742-4658.2009.07166.x · Cited by 42 · see citing works
RA-GEF-1, a Guanine Nucleotide Exchange Factor for Rap1, Is Activated by Translocation Induced by Association with Rap1·GTP and Enhances Rap1-dependent B-Raf Activation
Liao, Y., Satoh, T., Gao, X., Jin, T. J., Hu, C., & Kataoka, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101737200 · Cited by 63 · see citing works

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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