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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Epac is a Rap1 guanine-nucleotide-exchange factor directly activated by cyclic AMP

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FUNCTION AND REGULATION OF RAS

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cAMP Activates MAP Kinase and Elk-1 through a B-Raf- and Rap1-Dependent Pathway

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Rap1 mediates sustained MAP kinase activation induced by nerve growth factor

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Phospholipase Cϵ: a novel Ras effector

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Human RAS Superfamily Proteins and Related GTPases

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Signaling Specificity by Ras Family GTPases Is Determined by the Full Spectrum of Effectors They Regulate

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Differential Signaling of Cyclic AMP

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A growing family of guanine nucleotide exchange factors is responsible for activation of ras-family GTPases

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Rap1 Couples cAMP Signaling to a Distinct Pool of p42/44MAPK Regulating Excitability, Synaptic Plasticity, Learning, and Memory

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Ras GTPases: integrins' friends or foes?

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Identification of protein‐protein interactions using in vivo cross‐linking and mass spectrometry

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Cellular functions of the Rap1 GTP-binding protein: a pattern emerges

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Does Rap1 deserve a bad Rap?

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Ras and relatives—job sharing and networking keep an old family together

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Recognizing and Defining True Ras Binding Domains I: Biochemical Analysis

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Rap1-Mediated Activation of Extracellular Signal-Regulated Kinases by Cyclic AMP Is Dependent on the Mode of Rap1 Activation

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Rap1 up-regulation and activation on plasma membrane regulates T cell adhesion

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The Traf2- and Nck-interacting Kinase as a Putative Effector of Rap2 to Regulate Actin Cytoskeleton

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Regulating Rap small G-proteins in time and space

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Ras pathway signaling on endomembranes

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Rap1a Null Mice Have Altered Myeloid Cell Functions Suggesting Distinct Roles for the Closely Related Rap1a and 1b Proteins

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Functional coordination of alternative splicing in the mammalian central nervous system

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The RAP1 Guanine Nucleotide Exchange Factor Epac2 Couples Cyclic AMP and Ras Signals at the Plasma Membrane

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Differential roles of Ras and Rap1 in growth factor-dependent activation of phospholipase Cε

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Demonstration of Long-Range Interactions in a PDZ Domain by NMR, Kinetics, and Protein Engineering

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The Kinetics of PDZ Domain-Ligand Interactions and Implications for the Binding Mechanism

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Protein Kinase D1 and the β1 Integrin Cytoplasmic Domain Control β1 Integrin Function via Regulation of Rap1 Activation

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Characterisation of PDZ-GEFs, a family of guanine nucleotide exchange factors specific for Rap1 and Rap2

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Crucial Role of Phospholipase Cε in Skin Inflammation Induced by Tumor-Promoting Phorbol Ester

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Solution Structure of the PDZ2 Domain from Cytosolic Human Phosphatase hPTP1E Complexed with a Peptide Reveals Contribution of the β2–β3 Loop to PDZ Domain–Ligand Interactions

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BAG3 directly associates with guanine nucleotide exchange factor of Rap1, PDZGEF2, and regulates cell adhesion

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Crystal Structure of M-Ras Reveals a GTP-bound “Off” State Conformation of Ras Family Small GTPases

Ye, M., Shima, F., Muraoka, S., Liao, J., Okamoto, H., Yamamoto, M., Tamura, A., Yagi, N., Ueki, T., & Kataoka, T. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505503200 · Cited by 73

Crystallographic and Nuclear Magnetic Resonance Evaluation of the Impact of Peptide Binding to the Second PDZ Domain of Protein Tyrosine Phosphatase 1E

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Two conformational states of Ras GTPase exhibit differential GTP-binding kinetics

Liao, J., Shima, F., Araki, M., Ye, M., Muraoka, S., Sugimoto, T., Kawamura, M., Yamamoto, N., Tamura, A., & Kataoka, T. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.01.169 · Cited by 68

Non‐kinase second‐messenger signaling: new pathways with new promise

Springett, G. M., Kawasaki, H., & Spriggs, D. R. (2004) · BioEssays · doi:10.1002/bies.20057 · Cited by 68

Co-targeting SOS1 enhances the antitumor effects of KRASG12C inhibitors by addressing intrinsic and acquired resistance

Thatikonda, V., Lyu, H., Jurado, S., Kostyrko, K., Bristow, C. A., Albrecht, C., Alpar, D., Arnhof, H., Bergner, O., Bosch, K., et al. (2024) · Nature Cancer · doi:10.1038/s43018-024-00800-6 · Cited by 76

The PDZ-GEF Dizzy regulates cell shape of migrating macrophages via Rap1 and integrins in theDrosophilaembryo

Huelsmann, S., Hepper, C., Marchese, D., Knöll, C., & Reuter, R. (2006) · Development · doi:10.1242/dev.02449 · Cited by 59

The M-Ras-RA-GEF-2-Rap1 Pathway Mediates Tumor Necrosis Factor-α–dependent Regulation of Integrin Activation in Splenocytes

Yoshikawa, Y., Satoh, T., Tamura, T., Wei, P., Bilasy, S. E., Edamatsu, H., Aiba, A., Katagiri, K., Kinashi, T., Nakao, K., et al. (2007) · Molecular Biology of the Cell · doi:10.1091/mbc.e07-03-0250 · Cited by 61

MRAS: A Close but Understudied Member of the RAS Family

Young, L. C., & Rodriguez-Viciana, P. (2018) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a033621 · Cited by 53

Haplotypes spanning SPEC2, PDZ-GEF2 and ACSL6 genes are associated with schizophrenia

Chen, X., Wang, X., Hossain, S., O’Neill, F. A., Walsh, D., Pless, L., Chowdari, K. V., Nimgaonkar, V. L., Schwab, S. G., Wildenauer, D. B., et al. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl409 · Cited by 52

R-Ras3/M-Ras Induces Neuronal Differentiation of PC12 Cells through Cell-Type-Specific Activation of the Mitogen-Activated Protein Kinase Cascade

Kimmelman, A. C., Rodriguez, N. J. N., & Chan, A. M.-L. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.16.5946-5961.2002 · Cited by 54

The RapGEF PDZ-GEF2 is required for maturation of cell–cell junctions

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Aggregation of Lipid-Anchored Full-Length H-Ras in Lipid Bilayers: Simulations with the MARTINI Force Field

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MINK is a Rap2 effector for phosphorylation of the postsynaptic scaffold protein TANC1

Nonaka, H., Takei, K., Umikawa, M., Oshiro, M., Kuninaka, K., Bayarjargal, M., Asato, T., Yamashiro, Y., Uechi, Y., Endo, S., et al. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.10.038 · Cited by 47

Side-Chain Interactions Form Late and Cooperatively in the Binding Reaction between Disordered Peptides and PDZ Domains

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Peptide Binding to a PDZ Domain by Electrostatic Steering via Nonnative Salt Bridges

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PARG1, a protein-tyrosine phosphatase-associated RhoGAP, as a putative Rap2 effector

Myagmar, B., Umikawa, M., Asato, T., TAIRA, K., Oshiro, M., Hino, A., Takei, K., Uezato, H., & Kariya, K. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.02.069 · Cited by 39

Expression of activated M-Ras in a murine mammary epithelial cell line induces epithelial–mesenchymal transition and tumorigenesis

Ward, K. R., Zhang, K.-X., Somasiri, A. M., Roskelley, C. D., & Schrader, J. W. (2004) · Oncogene · doi:10.1038/sj.onc.1207226 · Cited by 40

M-Ras is activated by bone morphogenetic protein-2 and participates in osteoblastic determination, differentiation, and transdifferentiation

Watanabe‐Takano, H., Takano, K., Keduka, E., & Endo, T. (2009) · Experimental Cell Research · doi:10.1016/j.yexcr.2009.09.028 · Cited by 37

Insight into Catalysis of a Unique GTPase Reaction by a Combined Biochemical and FTIR Approach

Chakrabarti, P., Daumke, O., Suveyzdis, Y., Kötting, C., Gerwert, K. B., & Wittinghofer, A. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.11.022 · Cited by 37

M-Ras/Shoc2 signaling modulates E-cadherin turnover and cell–cell adhesion during collective cell migration

Kota, P. B., Terrell, E. M., Ritt, D. A., Insinna, C., Westlake, C. J., & Morrison, D. K. (2019) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1805919116 · Cited by 36

Critical Function of the Ras-associating Domain as a Primary Ras-binding Site for Regulation of Saccharomyces cerevisiaeAdenylyl Cyclase

Kido, M., Shima, F., Satoh, T., Asato, T., Kariya, K., & Kataoka, T. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109526200 · Cited by 36

Requirement of theCaenorhabditis elegansRapGEFpxf-1andrap-1for Epithelial Integrity

Berkel, W. P.-V., Verheijen, M. H. G., Cuppen, E. P. J. G., Asahina, M., de Rooij, J., Jansen, G., Plasterk, R. H. A., Bos, J. L., & Zwartkruis, F. J. T. (2004) · Molecular Biology of the Cell · doi:10.1091/mbc.e04-06-0492 · Cited by 35

Screening of hibernation-related genes in the brain of Rhinolophus ferrumequinum during hibernation

Chen, J., Yuan, L., Sun, M., Zhang, L., & Zhang, S. Y. (2007) · Comparative Biochemistry and Physiology Part B Biochemistry and Molecular Biology · doi:10.1016/j.cbpb.2007.10.011 · Cited by 30

Identification of a Novel Domain of Ras and Rap1 That Directs Their Differential Subcellular Localizations

Nomura, K., Kanemura, H., Satoh, T., & Kataoka, T. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314169200 · Cited by 30

Crucial Role of Rapgef2 and Rapgef6, a Family of Guanine Nucleotide Exchange Factors for Rap1 Small GTPase, in Formation of Apical Surface Adherens Junctions and Neural Progenitor Development in the Mouse Cerebral Cortex

Maeta, K., Edamatsu, H., Nishihara, K., Ikutomo, J., Bilasy, S. E., & Kataoka, T. (2016) · eNeuro · doi:10.1523/eneuro.0142-16.2016 · Cited by 30

Association of haplotypes spanning PDZ-GEF2, LOC728637 and ACSL6 with schizophrenia in Han Chinese

Luo, X.-J., Diao, H.-B., Wang, J.-K., Zhang, H., Zhao, Z. W., & Su, B. (2008) · Journal of Medical Genetics · doi:10.1136/jmg.2008.060657 · Cited by 28

Long-Range Conformational Response of a PDZ Domain to Ligand Binding and Release: A Molecular Dynamics Study

Lu, C., Knecht, V., & Stock, G. (2015) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.5b01009 · Cited by 29

Defective vascular morphogenesis and mid-gestation embryonic death in mice lacking RA-GEF-1

Wei, P., Satoh, T., Edamatsu, H., Aiba, A., Setsu, T., Terashima, T., Kitazawa, S., Nakao, K., Yoshikawa, Y., Tamada, M., et al. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.08.149 · Cited by 27

Novel Rap1 dominant-negative mutants interfere selectively with C3G and Epac

Dupuy, A. G., L'Hoste, S., Cherfils, J., Camonis, J., Gaudriault, G., & de Gunzburg, J. (2005) · Oncogene · doi:10.1038/sj.onc.1208647 · Cited by 26

Comprehensive behavioral analysis of mice deficient in Rapgef2 and Rapgef6, a subfamily of guanine nucleotide exchange factors for Rap small GTPases possessing the Ras/Rap-associating domain

Maeta, K., Hattori, S., Ikutomo, J., Edamatsu, H., Bilasy, S. E., Miyakawa, T., & Kataoka, T. (2018) · Molecular Brain · doi:10.1186/s13041-018-0370-y · Cited by 24

RA-GEF-1 (Rapgef2) is essential for proper development of the midline commissures

Bilasy, S. E., Satoh, T., Terashima, T., & Kataoka, T. (2011) · Neuroscience Research · doi:10.1016/j.neures.2011.08.004 · Cited by 22

M‐Ras induces Ral and JNK activation to regulate MEK/ERK‐independent gene expression in MCF‐7 breast cancer cells

Castro, A. F., Campos, T., Babcock, J. T., Armijo, M. E., Martínez‐Conde, A., Pincheira, R., & Quilliam, L. A. (2012) · Journal of Cellular Biochemistry · doi:10.1002/jcb.23458 · Cited by 22

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

Guo, X., Schrader, K. A., Xu, Y., & Schrader, J. W. (2005) · Oncogene · doi:10.1038/sj.onc.1208441 · Cited by 23

Deletion of Rapgef6, a candidate schizophrenia susceptibility gene, disrupts amygdala function in mice

Levy, R. J., Kvajo, M., Li, Y., Tsvetkov, E., Dong, W., Yoshikawa, Y., Kataoka, T., Bolshakov, V. Y., Karayiorgou, M., & Gogos, J. A. (2015) · Translational Psychiatry · doi:10.1038/tp.2015.75 · Cited by 19

M-Ras evolved independently of R-Ras and its neural function is conserved between mammalian and ascidian, which lacks classical Ras

Keduka, E., Kaiho, A., Hamada, M., Watanabe‐Takano, H., Takano, K., Ogasawara, M., Satou, Y., Satoh, N., & Endo, T. (2008) · Gene · doi:10.1016/j.gene.2008.10.001 · Cited by 19

Both knock-down and overexpression of Rap2a small GTPase in macrophages result in impairment of NF-κB activity and inflammatory gene expression

Carvalho, B. C., de Oliveira, L. C., Rocha, C. D., Fernandes, H. D. B., de Oliveira, I. M., Leão, F. B., Valverde, T. M., Rego, I. M. G., Ghosh, S., & Silva, A. M. (2019) · Molecular Immunology · doi:10.1016/j.molimm.2019.02.015 · Cited by 22

Rapid Protein–Ligand Affinity Determination by Photoinduced Hyperpolarized NMR

Bütikofer, M., Stadler, G. R., Kadavath, H., Cadalbert, R., Torres, F., & Riek, R. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c04000 · Cited by 17

Multiple Aspects of the Phenotype of Mammary Epithelial Cells Transformed by Expression of Activated M-Ras Depend on an Autocrine Mechanism Mediated by Hepatocyte Growth Factor/Scatter Factor

Zhang, K., Ward, K. R., & Schrader, J. W. (2004) · Molecular Cancer Research · doi:10.1158/1541-7786.242.2.4 · Cited by 16

M-RAS Regulate CDH1 Function in Blastomere Compaction during Porcine Embryonic Development

Zhou, D., Niu, Y., & Cui, X. (2020) · Journal of Animal Reproduciton and Biotechnology · doi:10.12750/jarb.35.1.12 · Cited by 14

Excitotoxic targeting of Kidins220 to the Golgi apparatus precedes calpain cleavage of Rap1-activation complexes

López‐Menéndez, C., Simón‐García, A., Gamir-Morralla, A., Pose‐Utrilla, J., Luján, R., Mochizuki, N., Díaz‐Guerra, M., & Iglesias, T. (2019) · Cell Death and Disease · doi:10.1038/s41419-019-1766-z · Cited by 15

M-Ras is Muscle-Ras, Moderate-Ras, Mineral-Ras, Migration-Ras, and Many More-Ras

Endo, T. (2020) · Experimental Cell Research · doi:10.1016/j.yexcr.2020.112342 · Cited by 14

Critical function of RA-GEF-2/Rapgef6, a guanine nucleotide exchange factor for Rap1, in mouse spermatogenesis

Okada, K., Miyake, H., Yamaguchi, K., Chiba, K., Maeta, K., Bilasy, S. E., Edamatsu, H., Kataoka, T., & Fujisawa, M. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.01.149 · Cited by 14

Impaired vascular development in the yolk sac and allantois in mice lacking RA-GEF-1

Kanemura, H., Satoh, T., Bilasy, S. E., Ueda, S., Hirashima, M., & Kataoka, T. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.07.108 · Cited by 14

A RAPGEF6 variant constitutes a major risk factor for laryngeal paralysis in dogs

Rasouliha, S. H., Barrientos, L., Anderegg, L., Klesty, C., Lorenz, J., Chevallier, L., Jagannathan, V., Rösch, S., & Leeb, T. (2019) · PLoS Genetics · doi:10.1371/journal.pgen.1008416 · Cited by 13

Identification of RARhoGAP, a novel putative RhoGAP gene expressed in male germ cells☆

Curry, B. J., Su, H., Law, E. G., McLaughlin, E. A., Nixon, B., & Aitken, R. J. (2004) · Genomics · doi:10.1016/j.ygeno.2004.03.004 · Cited by 13

Cytoplasmic Protein Serine/Threonine Kinases

Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_5 · Cited by 11

Signaling Lipids

Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_2 · Cited by 9

Gene Regulatory Network Analysis for Triple-Negative Breast Neoplasms by Using Gene Expression Data

Jung, H. C., Kim, S. H., Lee, J. H., Kim, J. H., & Han, S. W. (2017) · Journal of Breast Cancer · doi:10.4048/jbc.2017.20.3.240 · Cited by 10

Cytoplasmic Protein Tyrosine Kinases

Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_4 · Cited by 8

Guanosine Triphosphatases and Their Regulators

Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_9 · Cited by 7

The influence of MRAS gene variants on ischemic stroke and serum lipid levels in Chinese Han population

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Direct activation of fission yeast adenylyl cyclase by heterotrimeric G protein gpa2.

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Rapgef2, a guanine nucleotide exchange factor for Rap1 small GTPases, plays a crucial role in adherence junction (AJ) formation in radial glial cells through ERK-mediated upregulation of the AJ-constituent protein expression

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Transient recruitment of M-Ras GTPase to phagocytic cups in RAW264 macrophages during FcγR-mediated phagocytosis

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A road map for happiness: The psychological factors related cell types in various parts of human body from single cell RNA-seq data analysis

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Mitogen-Activated Protein Kinase Module

Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_6 · Cited by 5

Biochemistry of the Rap‐Specific Guanine Nucleotide Exchange Factors PDZ‐GEF1 and ‐2

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Role of R-Ras in Cell Growth

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Ras Family Proteins

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Dual-Specificity Protein Kinases

Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_7 · Cited by 2

Conclusion

Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_12 · Cited by 1

Cotargeting of Androgen Synthesis and Androgen Receptor Expression as a Novel Treatment for Castration-Resistant Prostate Cancer

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Preamble to Cytoplasmic Protein Kinases

Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_3

Does Rap1 mix and match

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Cytosolic Protein Phosphatases

Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_8

Other Major Types of Signaling Mediators

Thiriet, M. (2012) · Biomathematical and biomechanical modeling of the circulatory and ventilatory systems · doi:10.1007/978-1-4614-4370-4_10

Structural Analysis of Active Site Conformations in Ras and Rap1 GTPases.

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Targeting Neuroendocrine Differentiation for Prostate Cancer Radiosensitization

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The spatial control of Rap1 and Epac proteins

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Role of R-Ras in Cell Growth

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Structure and dynamics of the MAGUK core of PSD-95

Zhang, J. (2019) · Carolina Digital Repository (University of North Carolina at Chapel Hill) · doi:10.17615/wyec-7388

INTERACTOME REWIRING THROUGH CANCER-ASSOCIATED MUTATION IN GROWTH FACTOR SIGNALING PATHWAYS

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

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RA-GEF, a Novel Rap1A Guanine Nucleotide Exchange Factor Containing a Ras/Rap1A-associating Domain, Is Conserved between Nematode and Humans

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RasGEF1A and RasGEF1B are guanine nucleotide exchange factors that discriminate between Rap GTP‐binding proteins and mediate Rap2‐specific nucleotide exchange

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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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PDZ-GEF1, a Guanine Nucleotide Exchange Factor Specific for Rap1 and Rap2

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