The GTPase superfamily: conserved structure and molecular mechanism

Bourne, Henry R.; Sanders, David A.; McCormick, Frank

doi:10.1038/349117a0

Cited by 3,392Protein Kinase Regulation and GTPase SignalingReceptor Mechanisms and SignalingCellular transport and secretion

The GTPase superfamily: conserved structure and molecular mechanism

Bourne, Henry R., Sanders, David A., McCormick, Frank·1991·Nature

DOI 10.1038/349117a0

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Abstract

GTPases are conserved molecular switches, built according to a common structural design. Rapidly accruing knowledge of individual GTPases--crystal structures, biochemical properties, or results of molecular genetic experiments--support and generate hypotheses relating structure to function in other members of the diverse family of GTPases.

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Because G-proteins have intrinsically low GTPase activity, regulatory proteins are required for spatiotemporal control of the transition between active and inactive states.
“Rather, due to the intrinsically low GTPase activity of G-proteins, regulatory proteins are required for spatiotemporal control of the transition between active and inactive states (Fig. 1B).”
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GTPase affinity for guanine nucleotides is extremely high (Kd 10−7-10−11), ensuring committed states that do not spontaneously interchange and do not respond to changes in cellular nucleotide concentrations.
“The affinity of the interaction between GTPases and either guanine nucleotides is extremely high (Kd 10−7–10−11) ensuring that these are committed states that do not spontaneously interchange; they do not respond to changes in cellular nucleotide concentrations (8).”
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KRAS proteins primarily bind GDP and are in an inactive conformation maintained by intrinsic GTP hydrolytic activity.
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Amino acid sequence of mammalian elongation factor 2 deduced from the cDNA sequence: homology with GTP-binding proteins.
Kohno, K., Uchida, T., Ohkubo, H., Nakanishi, S., Nakanishi, T., Fukui, T., Ohtsuka, E., Ikehara, M., & Okada, Y. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.14.4978 · Cited by 138 · see citing works
Molecular cloning and sequence analysis of a ras gene from Schizosaccharomyces pombe.
Fukui, Y., & Kaziro, Y. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03684.x · Cited by 136 · see citing works
Coding sequence of humanrhocDNAs clone 6 and clone 9
Chardin, P., Madaule, P., & Tavitian, A. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.6.2717 · Cited by 136 · see citing works
Molecular cloning and sequence determination of the nuclear gene coding for mitochondrial elongation factor Tu of Saccharomyces cerevisiae.
Nagata, S., Tsunetsugu‐Yokota, Y., Naito, A., & Kaziro, Y. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.20.6192 · Cited by 134 · see citing works
Kinetic analysis of the hydrolysis of GTP by p21N-ras. The basal GTPase mechanism.
Neal, S. E., Eccleston, J. F., Hall, A., & Webb, M. R. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)77694-7 · Cited by 130 · see citing works
Characterization of transducin from bovine retinal rod outer segments. Participation of the amino-terminal region of T alpha in subunit interaction.
Navon, S. E., & Fung, B. K.-K. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)47791-5 · Cited by 128 · see citing works
A human homologue of the yeast GST1 gene codes for a GTP‐binding protein and is expressed in a proliferation‐dependent manner in mammalian cells.
Hoshino, S.-I., Miyazawa, H., Enomoto, T., Hanaoka, F., Kikuchi, Y., Kikuchi, A., & Ui, M. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08558.x · Cited by 122 · see citing works
A yeast gene required for the G1‐to‐S transition encodes a protein containing an A‐kinase target site and GTPase domain.
Kikuchi, Y., Shimatake, H., & Kikuchi, A. (1988) · The EMBO Journal · doi:10.1002/j.1460-2075.1988.tb02928.x · Cited by 119 · see citing works
Characterization and Developmental Expression of a Drosophila ras Oncogene
Mozer, B. A., Marlor, R. L., Parkhurst, S. M., & Corces, V. G. (1985) · Molecular and Cellular Biology · doi:10.1128/mcb.5.4.885-889.1985 · Cited by 115 · see citing works
Crystal structure of an active form of RAS protein, a complex of a GTP analog and the HRAS p21 catalytic domain.
Brünger, A. T., Milburn, M. V., Tong, L., Devos, A. M., Jancarik, J., Yamaizumi, Z., Nishimura, S., Ohtsuka, E., & Kim, S. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.12.4849 · Cited by 115 · see citing works
Saccharomyces cerevisiae and Schizosaccharomyces pombe contain a homologue to the 54-kD subunit of the signal recognition particle that in S. cerevisiae is essential for growth.
Hann, B. C., Poritz, M. A., & Walter, P. (1989) · The Journal of Cell Biology · doi:10.1083/jcb.109.6.3223 · Cited by 114 · see citing works
Identification of Small Clusters of Divergent Amino Acids that Mediate the Opposing Effects of ras and K rev -1
Zhang, K., Noda, M., Vass, W. C., Papageorge, A. G., & Lowy, D. R. (1990) · Science · doi:10.1126/science.2115210 · Cited by 111 · see citing works
Multiple alpha subunits of guanine nucleotide-binding proteins in Dictyostelium.
Pupillo, M., Kumagai, A., Pitt, G. S., Firtel, R., & Devreotes, P. N. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.13.4892 · Cited by 111 · see citing works
Hydrolysis of GTP by p21NRAS, the NRAS protooncogene product, is accompanied by a conformational change in the wild-type protein: use of a single fluorescent probe at the catalytic site.
Neal, S. E., Eccleston, J. F., & Webb, M. R. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.9.3562 · Cited by 109 · see citing works
Structure and expression of elongation factor 1α in tomato
Pokalsky, A. R., Hiatt, W. R., Ridge, N. P., Rasmussen, R. D., Houck, C. M., & Shewmaker, C. K. (1989) · Nucleic Acids Research · doi:10.1093/nar/17.12.4661 · Cited by 107 · see citing works
Sequence of the initiation factor IF2 gene: unusual protein features and homologies with elongation factors.
Sacerdot, C., Dessen, P., Hershey, J. W. B., PLUMBRIDGE, J. A., & GRUNBERG‐MANAGO, M. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.24.7787 · Cited by 107 · see citing works
Molecular cloning, characterization, and expression of human ADP-ribosylation factors: two guanine nucleotide-dependent activators of cholera toxin.
Bobak, D. A., Nightingale, M. S., Murtagh, J. J., Price, S. R., Moss, J., & Vaughan, M. J. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.16.6101 · Cited by 107 · see citing works
The nucleotide sequence of an Escherichia coli operon containing genes for the tRNA(m1G)methyltransferase, the ribosomal proteins S16 and L19 and a 21‐K polypeptide.
Byström, A. S., Hjalmarsson, K., Wikström, P. M., & Björk, G. R. (1983) · The EMBO Journal · doi:10.1002/j.1460-2075.1983.tb01519.x · Cited by 107 · see citing works
The amino terminus of G protein alpha subunits is required for interaction with beta gamma.
Neer, E. J., Pulsifer, L., & Wolf, L. G. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68406-6 · Cited by 103 · see citing works
Identification of the ral and rac1 Gene Products, Low Molecular Mass GTP-binding Proteins from Human Platelets
Polakis, P. G., Weber, R. F., Nevins, B., Didsbury, J. R., Evans, T., & D, R. S. M. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84717-8 · Cited by 102 · see citing works
A role for Ni in the hormonal stimulation of adenylate cyclase
Cerione, R. A., Staniszewski, C., Caron, M. G., Lefkowitz, R. J., Codina, J., & Birnbaumer, L. (1985) · Nature · doi:10.1038/318293a0 · Cited by 100 · see citing works
Xenopus oocyte germinal-vesicle breakdown induced by [Val12]Ras is inhibited by a cytosol-localized Ras mutant.
Gibbs, W. W., Schaber, M. D., Schofield, T. L., Scolnick, E. M., & Sigal, I. S. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.17.6630 · Cited by 99 · see citing works
Reactive sulfhydryl groups of alpha 39, a guanine nucleotide-binding protein from brain. Location and function.
Winslow, J. W., Bradley, J. D., Smith, J. A., & Neer, E. J. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61220-7 · Cited by 97 · see citing works
Organization and codon usage of the streptomycin operon in Micrococcus luteus, a bacterium with a high genomic G + C content
Ohama, T., Yamao, F., Muto, A., & Osawa, S. (1987) · Journal of Bacteriology · doi:10.1128/jb.169.10.4770-4777.1987 · Cited by 93 · see citing works
Sequence analysis of bovine retinal S‐antigen
Wistow, G. J., Katial, A., Craft, C. M., & Shinohara, T. (1986) · FEBS Letters · doi:10.1016/0014-5793(86)80207-1 · Cited by 92 · see citing works
The Mechanism of Guanosine Nucleotide Hydrolysis by p21 c-Ha-ras
Feuerstein, J., Goody, R. S., & Webb, M. R. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83331-2 · Cited by 90 · see citing works
The nucleotide sequence of theEscherichta coli fusgene, coding for elongation factor G
Zengel, J. M., Archer, R. H., & Lindahl, L. (1984) · Nucleic Acids Research · doi:10.1093/nar/12.4.2181 · Cited by 88 · see citing works
Cloning of ara, a putative Arabidopsis thaliana gene homologous to the ras-related gene family
Matsui, M., Sasamoto, S., Kunieda, T., Nomura, N., & Ishizaki, R. (1989) · Gene · doi:10.1016/0378-1119(89)90171-6 · Cited by 86 · see citing works
Ras interaction with the GTPase‐activating protein (GAP)
Schaber, M. D., Garsky, V. M., Boylan, D., Hill, W. S., Scolnick, E. M., Marshall, M. S., Sigal, I. S., & Gibbs, W. W. (1989) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340060313 · Cited by 82 · see citing works
Characterization of the lep operon of Escherichia coli. Identification of the promoter and the gene upstream of the signal peptidase I gene.
March, P. E., & Inouye, M. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)39594-7 · Cited by 80 · see citing works
The amino acid sequence of elongation factor Tu of Escherichia coli. The complete sequence.
Laursen, R. A., L'Italien, J. J., Nagarkatti, S., & Miller, D. L. (1981) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)43394-7 · Cited by 77 · see citing works
Mechanism of action of monoclonal antibodies that block the light activation of the guanyl nucleotide-binding protein, transducin.
Hamm, H. E., Deretic, D., Hofmann, K., Schleicher, A., & Kohl, B. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61039-7 · Cited by 69 · see citing works
Molecular cloning and sequence determination of the tuf gene coding for the elongation factor Tu of Thermus thermophilus HB8
Kushiro, A., Shimizu, M., & Tomita, K.-I. (1987) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1987.tb13671.x · Cited by 66 · see citing works
Cloning and nucleotide sequence of the gene for an archaebacterial protein synthesis elongation factor Tu
Lechner, K., & Böck, A. (1987) · Molecular and General Genetics MGG · doi:10.1007/bf00328150 · Cited by 66 · see citing works
Topographic analysis of antigenic determinants recognized by monoclonal antibodies to the photoreceptor guanyl nucleotide-binding protein, transducin.
Deretic, D., & Hamm, H. E. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)61040-3 · Cited by 65 · see citing works
Biochemical and crystallographic characterization of a complex of c-Ha-ras p21 and caged GTP with flash photolysis.
Schlichting, I., Rapp, G., John, J., Wittinghofer, A., PAI, E. F., & Goody, R. S. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.20.7687 · Cited by 65 · see citing works
Expression of an activated ras gene causes developmental abnormalities in transgenic Drosophila melanogaster.Preprint
Bishop, J. G., & Corces, V. G. (1988) · Genes & Development · doi:10.1101/gad.2.5.567 · Cited by 61 · see citing works
Characterization of the str operon genes from Spirulina platensis and their evolutionary relationship to those of other prokaryotes
Buttarelli, F. R., Calogero, R., Tiboni, O., Gualerzi, C. O., & Pon, C. L. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf00330947 · Cited by 60 · see citing works
Characterization of functional domains of p21 ras by use of chimeric genes.
Schejter, E. D., & Shilo, B. (1985) · The EMBO Journal · doi:10.1002/j.1460-2075.1985.tb03643.x · Cited by 59 · see citing works
Conformational changes involved in the activation of ras p21: Implications for related proteins
JURNAK, F. A., Heffron, S. E., & Bergmann, E. M. (1990) · Cell · doi:10.1016/0092-8674(90)90652-u · Cited by 59 · see citing works
Mechanism of the Nucleotide Exchange Reaction in Eukaryotic Polypeptide Chain Initiation
Dholakia, J. N., & Wahba, A. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)31293-0 · Cited by 57 · see citing works
Studies on the Polypeptide Elongation Factors from E. coli
Arai, K., Kawakita, M., NAKAMURA, S., ISHIKAWA, I., & Kaziro, Y. (1974) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a130596 · Cited by 55 · see citing works
Kinetics and thermodynamics of the interaction of elongation factor Tu with elongation factor Ts, guanine nucleotides, and aminoacyl-tRNA.
Romero, G. G., Chau, V., & Biltonen, R. L. (1985) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)88952-9 · Cited by 52 · see citing works
Characterization of transducin from bovine retinal rod outer segments. Use of monoclonal antibodies to probe the structure and function of the subunit.
Navon, S. E., & Fung, B. K.-K. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)57419-1 · Cited by 52 · see citing works
A new RAS mutation that suppresses the CDC25 gene requirement for growth of Saccharomyces cerevisiae.
Camonis, J., & Jacquet, M. (1988) · Molecular and Cellular Biology · doi:10.1128/mcb.8.7.2980 · Cited by 52 · see citing works
A new member of therasgene superfamily identified in a rat liver cell line
Bucci, C., Frunzio, R., Chiariotti, L., Brown, A. L., Rechler, M. M., & Bruni, C. B. (1988) · Nucleic Acids Research · doi:10.1093/nar/16.21.9979 · Cited by 51 · see citing works
Genes for the ribosomal proteins S12 and S7 and elongation factors EF-G and EF-Tu of the cyanobacterium, Anacystis nidulans: Structural homology between 16S rRNA and S7 mRNA
Meng, B. Y., Shinozaki, K., & Sugiura, M. (1989) · Molecular and General Genetics MGG · doi:10.1007/bf00332226 · Cited by 51 · see citing works
Expression of a Gαs/Gαi Chimera That Constitutively Activates Cyclic AMP Synthesis
Woon, C.-W., Soparkar, S., Heasley, L. E., & Johnson, G. L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83603-1 · Cited by 45 · see citing works
Mutagenesis of bacterial elongation factor Tu at lysine 136
Hwang, Y., Sanchez, A., & Miller, D. L. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)83183-0 · Cited by 42 · see citing works
Nucleotide sequence of the gene coding for the elongation factor Tu from the extremely thermophilic eubacterium Thermotoga maritima
Bachleitner, M. (1989) · FEMS Microbiology Letters · doi:10.1016/0378-1097(89)90157-2 · Cited by 40 · see citing works
Hydrolysis of GTP by the α‐chain of Gs and other GTP binding proteins
Bourne, H. R., Landis, C. A., & Masters, S. B. (1989) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.340060304 · Cited by 37 · see citing works
Self-citation
The Guanine - Nucleotide Binding Proteins: Common Structural And Functional Properties
Properties, F., Bosch, L. V. D., Kraal, B., & Parmeggiani, A. (2013) · Cited by 36 · see citing works
Nucleotide sequence of the gene coding for the elongation factor Tu from the extremely thermophilic eubacteriumThermotoga maritima
Bachleitner, M., Ludwig, W., STETTER, K. O., & Schleifer, H. (1989) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.1989.tb03231.x · Cited by 34 · see citing works
Chimeric proteins define variable and essential regions of Ha-ras-encoded protein.
Lowe, D. G., Ricketts, M., Levinson, A. D., & Goeddel, D. V. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.4.1015 · Cited by 30 · see citing works
Conformation change of effector-region residues in antiparallel β-sheet of human c-Ha-ras protein on GDP→GTPγS exchange: A two-dimensional NMR study
Yamasaki, K., Kawai, G., Ito, Y., Muto, Y., Fujita‐Yoshigaki, J., Miyazawa, T., Nishimura, S., & Yokoyama, S. (1989) · Biochemical and Biophysical Research Communications · doi:10.1016/0006-291x(89)90780-8 · Cited by 30 · see citing works
Structure and expression of elongation factor 2 gene during development of Dictyostelium discoideum
Toda, K., Tasaka, M., Mashima, K., Kohno, K., Uchida, T., & Takeuchi, I. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84856-1 · Cited by 30 · see citing works
Diverse Biological Functions of Small GTP-binding Proteins in YeastPreprint
Botstein, D., Segev, N., Stearns, T., Hoyt, M. A., Holden, J., & Kahn, R. (1988) · Cold Spring Harbor Symposia on Quantitative Biology · doi:10.1101/sqb.1988.053.01.072 · Cited by 30 · see citing works
Antibodies to Synthetic Peptide from the Residue 33 to 42 Domain of c-Ha- ras p21 Block Reconstitution of the Protein with Different Effectors
Rey, I., Soubigou, P., Debüssche, L., David, C., Morgat, A., Bost, P., Mayaux, J. F., & Tocqué, B. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3904-3910.1989 · Cited by 23 · see citing works
H- ras Mutants Lacking the Epitope for the Neutralizing Monoclonal Antibody Y13-259 Show Decreased Biological Activity and Are Deficient in GTPase-Activating Protein Interaction
Srivastava, S. K., Donato, A. D., & Lacal, J. C. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.4.1779-1783.1989 · Cited by 21 · see citing works
Identification, cloning and sequence of the Streptococcus faecium infB (translational initiation factor IF2) gene
FRIEDRICH, K., Brombach, M., & Pon, C. L. (1988) · Molecular and General Genetics MGG · doi:10.1007/bf00330501 · Cited by 20 · see citing works
A Mutation That Hinders The GTP Induced Aminoacyl-tRNA BINDING of ELONGATION Factor TU
Hwang, Y., JURNAK, F. A., & Miller, D. L. (1989) · Springer eBooks · doi:10.1007/978-1-4757-2037-2_8 · Cited by 16 · see citing works
Genes encoding novel GTP‐binding proteins in Dictyostelium
Saxe, S. A., & Kimmel, A. R. (1988) · Developmental Genetics · doi:10.1002/dvg.1020090408 · Cited by 10 · see citing works
G Proteins in Yeast Saccharomyces cerevisiae
Kurjan, J. (1990) · Elsevier eBooks · doi:10.1016/b978-0-12-377450-7.50028-9 · Cited by 3 · see citing works

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The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
Ridley, A. J., Paterson, H. F., Johnston, C. L., Diekmann, D., & Hall, A. (1992) · Cell · doi:10.1016/0092-8674(92)90164-8 · Cited by 3,651 · see citing works
Mammalian Mitogen-Activated Protein Kinase Signal Transduction Pathways Activated by Stress and Inflammation
Kyriakis, J. M., & Avruch, J. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.2.807 · Cited by 3,369 · see citing works
Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
Chen, H., Detmer, S. A., Ewald, A. J., Griffin, E. E., Fraser, S. E., & Chan, D. C. (2003) · The Journal of Cell Biology · doi:10.1083/jcb.200211046 · Cited by 2,601 · see citing works
Small GTP-Binding Proteins
Takai, Y., Sasaki, T., & Matozaki, T. (2001) · Physiological Reviews · doi:10.1152/physrev.2001.81.1.153 · Cited by 2,466 · see citing works
Identification of FAP Locus Genes from Chromosome 5q21
Kinzler, K. W., Nilbert, M. C., Su, L.-K., Vogelstein, B., Bryan, T. M., Levy, D. B., Smith, K. J., Preisinger, A. C., Hedge, P., McKechnie, D., et al. (1991) · Science · doi:10.1126/science.1651562 · Cited by 2,331 · see citing works
Diversity of G Proteins in Signal Transduction
Simon, M. I., Strathmann, M., & Gautam, N. (1991) · Science · doi:10.1126/science.1902986 · Cited by 2,016 · see citing works
Mammalian Ras interacts directly with the serine/threonine kinase Raf.
Vojtek, A., Hollenberg, S., & Cooper, J. A. (1993) · Cell · doi:10.1016/0092-8674(93)90307-c · Cited by 1,971 · see citing works
Proteins regulating Ras and its relatives
Boguski, M. S., & McCormick, F. P. (1993) · Nature · doi:10.1038/366643a0 · Cited by 1,905 · see citing works
Self-citation
The small GTP-binding proteins Rac1 and Cdc42regulate the activity of the JNK/SAPK signaling pathway
Coso, O. A., Chiariello, M., Yu, J., Teramoto, H., Crespo, P., Xu, N., Miki, T., & Gutkind, J. S. (1995) · Cell · doi:10.1016/s0092-8674(05)80018-2 · Cited by 1,629 · see citing works
Genome-Wide Analysis of NBS-LRR–Encoding Genes in Arabidopsis[W]
Meyers, B. C., Kozik, A., Griego, A., Kuang, H., & Michelmore, R. W. (2003) · The Plant Cell · doi:10.1105/tpc.009308 · Cited by 1,605 · see citing works
The Ras-RasGAP Complex: Structural Basis for GTPase Activation and Its Loss in Oncogenic Ras Mutants
Scheffzek, K., Ahmadian, M. R., Kabsch, W., Wiesmüller, L., Lautwein, A., Schmitz, F., & Wittinghofer, A. (1997) · Science · doi:10.1126/science.277.5324.333 · Cited by 1,543 · see citing works
Hyperactive Ras in developmental disorders and cancer
Schubbert, S., Shannon, K., & Bollag, G. (2007) · Nature Reviews Cancer · doi:10.1038/nrc2109 · Cited by 1,583 · see citing works
The Ras superfamily at a glance
Wennerberg, K., Rossman, K. L., & Der, C. J. (2005) · Journal of Cell Science · doi:10.1242/jcs.01660 · Cited by 1,549 · see citing works
The small GTPase rab5 functions as a regulatory factor in the early endocytic pathway
Bucci, C., Parton, R. G., Mather, I. H., Stunnenberg, H. G., Simons, K., Hoflack, B., & Zerial, M. (1992) · Cell · doi:10.1016/0092-8674(92)90306-w · Cited by 1,370 · see citing works
G Protein Pathways
Neves, S. R., Ram, P. T., & Iyengar, R. (2002) · Science · doi:10.1126/science.1071550 · Cited by 1,300 · see citing works
Uncovering Molecular Mechanisms Involved in Activation of G Protein-Coupled Receptors
Gether, U. (2000) · Endocrine Reviews · doi:10.1210/edrv.21.1.0390 · Cited by 1,264 · see citing works
Association of Sos Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
Egan, S. E., Giddings, B. W., Brooks, M. W., Buday, L., Sizeland, A. M., & Weinberg, R. A. (1993) · Nature · doi:10.1038/363045a0 · Cited by 1,200 · see citing works
A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex.
Matunis, M. J., Coutavas, E. E., & Blobel, G. (1996) · The Journal of Cell Biology · doi:10.1083/jcb.135.6.1457 · Cited by 1,199 · see citing works
Insights into protein-protein binding by binding free energy calculation and free energy decomposition for the Ras-Raf and Ras-RalGDS complexes.
Gohlke, H., Kiel, C., & Case, D. (2003) · Journal of Molecular Biology · doi:10.1016/s0022-2836(03)00610-7 · Cited by 1,087 · see citing works
Classification and evolution of P-loop GTPases and related ATPases
Leipe, D. D., Wolf, Y. I., Koonin, E. V., & Aravind, L. (2002) · Journal of Molecular Biology · doi:10.1006/jmbi.2001.5378 · Cited by 1,148 · see citing works
KRAS Mutation: From Undruggable to Druggable in Cancer
Huang, L., Guo, Z., Wang, F., & Fu, L. (2021) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-021-00780-4 · Cited by 1,127 · see citing works
The structure of the G protein heterotrimer Giα1β1γ2
Wall, M. A., Coleman, D. E., Lee, E. N., Iñiguez-Lluhı́, J. A., Posner, B. A., Gilman, A. G., & Sprang, S. R. (1995) · Cell · doi:10.1016/0092-8674(95)90220-1 · Cited by 1,134 · see citing works
G PROTEIN MECHANISMS: Insights from Structural Analysis
Sprang, S. R. (1997) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.66.1.639 · Cited by 1,057 · see citing works
Glucosylation of Rho proteins by Clostridium difficile toxin B
Just, I., Selzer, J., Wilm, M. S., von Eichel-Streiber, C., Mann, M., & Aktories, K. (1995) · Nature · doi:10.1038/375500a0 · Cited by 1,032 · see citing works
Control of mitochondrial morphology by a human mitofusin
Santel, A., & Fuller, M. T. (2001) · Journal of Cell Science · doi:10.1242/jcs.114.5.867 · Cited by 1,012 · see citing works
Co-purification and Direct Interaction of Ras with Caveolin, an Integral Membrane Protein of Caveolae Microdomains
Song, K. S., Li, S. C., Okamoto, T., Quilliam, L. A., Sargiacomo, M., & Lisanti, M. P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.16.9690 · Cited by 1,000 · see citing works
Distinct morphogenetic functions of similar small GTPases: Drosophila Drac1 is involved in axonal outgrowth and myoblast fusion.Preprint
Luo, L.-Q., Liao, Y.-J., Jan, L., & Jan, Y. (1994) · Genes & Development · doi:10.1101/gad.8.15.1787 · Cited by 1,036 · see citing works
Association of the Shc and Grb2/Sem5 SH2-containing proteins is implicated in activation of the Ras pathway by tyrosine kinases
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Authors: Bourne, H. R., Sanders, D. A., & McCormick, F.
Affiliations: University of California, San Francisco (US)
Whitehead Institute for Biomedical Research (US)
ORCID: Sanders, David A.
McCormick, Frank
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 1991-01-10
Volume: 349
Issue: 6305
Pages: 117-127
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/349117a0
OpenAlex: W1977598234
Cited by: 3,392
References: 149
Citations by year: 2026: 24 · 2025: 44 · 2024: 51 · 2023: 52 · 2022: 37 · 2021: 55 · 2020: 62 · 2019: 50 · 2018: 48 · 2017: 44 · 2016: 58 · 2015: 56 · 2014: 63 · 2013: 61 · 2012: 69
FWCI: 30.15
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Nature (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 › Receptor Mechanisms and Signaling
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Cellular transport and secretion
Keywords: GTPase, GTPase superfamily, molecular switches, structure-function relationship, molecular mechanisms, crystal structure, molecular genetics
MeSH terms: Amino Acid Sequence, Animals, Guanosine Diphosphate, Guanosine Triphosphate, Humans, Molecular Sequence Data, Peptide Elongation Factors, Peptide Initiation Factors, Protein Conformation, Protein Processing, Post-Translational, Signal Transduction, Proto-Oncogene Proteins p21(ras), GTP-Binding Proteins, GTP Phosphohydrolase-Linked Elongation Factors

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The GTPase superfamily: conserved structure and molecular mechanism

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