-
4
-
-
0026778133
-
The Small GTP-Binding Protein Rho Regulates the Assembly of Focal Adhesion and Actin Stress Fibers in Response to Growth Factors
-
(1992)
Cell
, vol.70
, pp. 389-399
-
-
Ridley1
Hall2
-
6
-
-
0027525103
-
Friends and Family: the Role of the Rab GTPases in Vesicular Traffic
-
(1993)
Cell
, vol.75
, pp. 597-602
-
-
Novick1
Brennwald2
-
9
-
-
0025789103
-
Premature Initiation of Mitosis in Yeast Lacking RCC1 or an Interacting GTPase
-
(1991)
Cell
, vol.66
, pp. 347-360
-
-
Matsumoto1
Beach2
-
10
-
-
0027376308
-
The GTP Binding Protein Rank/TC4 is Required for Protein Import into the Nucleus
-
(1993)
Nature
, vol.365
, pp. 661-663
-
-
Moore1
Blobel2
-
13
-
-
0025295180
-
Purification and Characterization from Bovine Brain Cytosol of a Novel Regulatory Protein Inhibiting the Dissociation of GDP from and Subsequent Binding of GTP to RhoB p20, a Ras-p21 Like GTP-Binding Protein
-
(1990)
J Biol Chem
, vol.265
, pp. 9373-9380
-
-
Ueda1
Kikuchi2
Ohga3
Yamamoto4
Takai5
-
15
-
-
0027465064
-
Epidermal Growth Factor Regulates the Exchange Rate of Guanine Nucleotides on p21rs in Fibroblasts
-
of special interest, This paper uses the same technique as [14⊎] and comes to the same conclusions. Increased guanine-nucleotide exchange activity appears to be responsible for the elevated percentage of Ras bound to GTP observed after growth factor stimulation.
-
(1993)
Mol Cell Biol
, vol.13
, pp. 1903-1910
-
-
Buday1
Downward2
-
22
-
-
0025997867
-
Ras1 and a Putative Guanine Nucleotide Exchange Factor Perform Crucial Steps in Signaling by the Sevenless Protein Tyrosine Kinase
-
(1991)
Cell
, vol.67
, pp. 701-716
-
-
Simon1
Bowtell2
Dodson3
Lavety4
Rubin5
-
23
-
-
0026608238
-
The Son of Sevenless Gene Product: A Putative Activator of Ras
-
of outstanding interest, This group used mapping techniques to clone SOS and find that the amino sequence it encoded was similar to that of the yeast CDC25 Ras exchange factor. As in [22], the proline-rich tail of SOS revealed from its DNA sequence suggested it could bind the SH3 domain of Grb2/Sem5/Drk.
-
(1992)
Science
, vol.255
, pp. 603-605
-
-
Bonfini1
Karlovich2
Dasgupta3
Banerjee4
-
24
-
-
0027401746
-
DSS4-1 is A Dominant Suppressor of Sec4–8 that Encodes A Nucleotide Exchange Protein that Aids Sec4p Function
-
of special interest, The cloning of the first Rab nucleotide exchange factor by selection of a gene in yeast that can overcome a temperature-sensitive mutation in the sec4 GTPase. This GEF is unique in that it is only 17 kDa in size.
-
(1993)
Nature
, vol.361
, pp. 460-463
-
-
Moya1
Roberts2
Novick3
-
25
-
-
0027500969
-
SEC12 Encodes A Guanine-Nucleotide Exchange Factor Essential for Transport Vesicle Budding from the ER
-
of special interest, This gene was first cloned as a result of interest in the fact that its deletion from the genome inhibits vesicle budding from the endoplasmic reticulum. Biochemical assays of a soluble 40 kDa protein expressed in yeast revealed GEF activity against Sar1, a member of the Rab GTPase subfamily.
-
(1993)
Nature
, vol.365
, pp. 347-349
-
-
Barlowe1
Schekman2
-
26
-
-
0026523616
-
Cloning by Functional Complementation of a Mouse cDNA Encoding a Homologue of CDC25, a Saccharomyces cerevisiae RAS Activator
-
of special interest, This group used complementation of a defective yeast strain lacking the yeast RAS CDC25 gene to clone a piece of a mouse gene with the potential to activate Ras. The gene is the same as the rat Ras-GRF described in [28⊎,64].
-
(1992)
EMBO J
, vol.11
, pp. 2151-2157
-
-
Marṫegani1
Vanoni2
Zippel3
Coccetti4
Brambilla5
Ferrari6
Sturani7
Alberghina8
-
27
-
-
0027417269
-
A Mammalian Guanine-Nucleotide-Releasing Protein Enhances Function by Yeast Secretory Protein Sec4
-
of special interest, A mammalian homologue of the yeast Dss4 gene was cloned by its ability to rescue a Dss4 minus strain of yeast. This GEF had the ability to promote GDP release from the mammalian Rab3A protein. Given that there are over 30 Rab family members, it will be interesting to see how many Rab GEFs there are and how specific each one is.
-
(1993)
Nature
, vol.361
, pp. 464-467
-
-
Burton1
Roberts2
Montaldi3
Novick4
-
28
-
-
0026659515
-
Molecular Cloning of cDNAs Encoding A Guanine-Nucleotide Releasing Factor for Ras p21
-
of special interest, By predicting amino acid residues that would be expected to be conserved from yeast to mammals, mixed oligonucleotide PCR was used to clone a rat gene encoding a 140 kDa mammalian Ras-GEF (or GRF). The conserved catalytic domain was shown to activate Ras in vitro. Moreover, a Dbl-homology domain was observed at the amino end of the protein, suggesting this protein might activate a second member of the Ras superfamily. Finally, expression of the gene was detected only in brain.
-
(1992)
Nature
, vol.358
, pp. 351-354
-
-
Shou1
Farnsworth2
Neel3
Feig4
-
29
-
-
0026695971
-
Identification of a Mammalian Gene Structurally and Functionally Related to the CDC25 Gene of Sacchromyces cerevisiea
-
of special interest, Mixed oligonucleotide PCR, using residues conserved in yeast RAS-GEFs, was used to clone a piece of mammalian Ras-GEF. The gene is the same as the encoding Ras-GRF, and is described in [28⊎,64].
-
(1992)
Proc Natl Acad Sci USA
, vol.89
, pp. 7100-7104
-
-
Wei1
Mosteller2
Sanyal3
Gonzales4
McKinney5
Dasgupta6
Li7
Liu8
Broek9
-
30
-
-
0026627960
-
Identification of Murine Homologues of the Drosophila Son of Sevenless Gene: Potential Activators of Ras
-
of special interest, Low stringency hybridization of a mouse cDNA library, using Drosophila SOS, allowed the cloning of two mammalian homologues, mSOS-1 and mSOS-2. In addition to a conserved Ras-activating domain, the encoded protein also contained the proline-rich carboxyl terminus, which suggested that mSOS binds the adaptor Grb2 in mammalian cells.
-
(1992)
Proc Natl Acad Sci USA
, vol.89
, pp. 6511-6515
-
-
Bowtell1
Fu2
Simon3
Senior4
-
31
-
-
0027207287
-
Tyrosine Kinase-Stimulated Guanine Nucleotide Exchange Activity of Vav in T Cell Activation
-
of outstanding interest, Vav was shown to be an exchange factor for Ras in T cells. This was a remarkable result because Vav has a domain similar to the catalytic domain of Dbl, which is a GEF for Rho family members RhoA and CDC42. Vav GEF activity was enhanced by tyrosine phosphorylation.
-
(1993)
Science
, vol.260
, pp. 822-825
-
-
Gulbins1
Coggeshall2
Baier3
Katzav4
Burn5
Altman6
-
33
-
-
0026419320
-
Catalysis of Guanine Nucleotide Exchange on Ran by the Mitotic Regulator RCC1
-
(1991)
Nature
, vol.354
, pp. 80-82
-
-
Bischoff1
Ponstingl2
-
34
-
-
0027413917
-
RCC1 in the Cell Cycle: the Regulator of Chromosome Condensation Takes on New Roles
-
(1993)
Trends Biochem Sci
, vol.18
, pp. 96-101
-
-
Dasso1
-
35
-
-
0026677375
-
Brefeldin A Inhibits Golgi Membrane-Catalysed Exchange of Guanine Nucleotide in ARF Protein
-
(1992)
Nature
, vol.36
, pp. 350-352
-
-
Donaldson1
Finazzi2
Klausner3
-
36
-
-
0026746713
-
Inhibition by Brefeldin A of a Golgi Membrane Enzyme that Catalyzes Exchange of Guanine Nucleotide Bound to ARE
-
(1992)
Nature
, vol.360
, pp. 352-354
-
-
Helms1
Rothman2
-
38
-
-
0026608178
-
C. Elegans Cell-Signalling Gene Sem-5 Encodes a Protein with SH2 and SH3 Domains
-
of outstanding interest, This paper was one in a series that exploited the ‘elegance’ of C. elegans to identify components of a Ras signalling pathway that are involved in development. This particular paper had a major impact on the signal transduction field, because it argued that an adaptor protein (Sem5), containing only SH2 and SH3 domains, functioned between tyrosine kinase receptors and Ras. Its amino acid sequence immediately suggested a function for the independently cloned human and rat homologues, Grb2/Ash.
-
(1992)
Nature
, vol.356
, pp. 340-344
-
-
Clark1
Stern2
Horvitz3
-
39
-
-
0026729382
-
The SH2 and SH3 Domain-Containing protein GRB2 Links Receptor Tyrosine Kinases to Ras Signallin
-
of special interest, This paper described the cloning of Grb2 on the basis of its SH2 domain's ability to bind a tyrosine-phosphorylated receptor. It also gave the first functional hint that Grb2, the mammalian homologue of C. elegans Sem5, functions in transmitting signals from tyrosine kinase receptors.
-
(1992)
Cell
, vol.70
, pp. 431-442
-
-
Lowenstein1
Daly2
Batzer3
Li4
Margolis5
Lammers6
Ullrich7
Skolnik8
Bar-Sagi9
Schlessinger10
-
41
-
-
0026743906
-
Identification of a protein that Binds to the SH3 Region of Abl and is Similar to Bcr and GAP-Rho
-
of outstanding interest, This paper had a tremendous influence on the signal transduction field because it was the first to characterize sites on the protein that are recognized by SH3 domains. For the Ras field these results led to the prediction and subsequent confirmation that the proline-rich carboxy-terminal tail of SOS could bind the SH3 domain of Grb2.
-
(1992)
Nature
, vol.257
, pp. 803-806
-
-
Cichetti1
Mayer2
Thiel3
Baltimore4
-
42
-
-
0027468233
-
A Drosophila SH2–SH3 Adaptor Protein Implicated ini Coupling the Sevenless Tyrosine Kinase to An Activator of Ras Guanine Nucleotide Exchange, SOS
-
of special interest, This paper and [43⊎] analyze tyrosine kinase receptor, adaptor protein and Ras exchange factor interpretations in eye development in Drosophila. The authors show evidence for interactions between an EGF-like receptor, Drk (Grb2 homologue) and SOS, that are analogous to those that take place between similar proteins in mammalian cells.
-
(1993)
Cell
, vol.73
, pp. 179-191
-
-
Olivier1
Raabe2
Henkemeyer3
Dickson4
Mbamalu5
Margolis6
Schlessinger7
Hafen8
Pawson9
-
43
-
-
0027404990
-
An SH3-SH2-SH3 Protein is Required for p21ras1 Activation and Binds too Sevenless and SOS Proteins in Vitro
-
of special interest, Isolation of a Sem5/Grb2 homologue from Drosophila and a demonstration that it connects a tyrosine kinase receptor to the Ras activator protein, SOS. This paper and [42⊎] dramatize how the pathway from tyrosine kinase receptors to Ras has been conserved during evolution.
-
(1993)
Cell
, vol.73
, pp. 169-177
-
-
Simon1
Dodson2
Rubin3
-
44
-
-
0027153103
-
Epidermal Growth Factor Regulates p21Ras Through the Formation of a Complex of Receptor, Grb2 Adaptor Protein, and SOS Nucleotide Exchange Factor
-
of special interest, One of six papers [16,44⊎–48⊎] that came out at about the same time showing that the activation of the EGF receptor leads to formation of a complex between the receptor, the adaptor protein, Grb2, and the Ras activator, mSOS. This paper was unique in that is showed no change in specific GEF activity of SOS after growth factor stimulation of cells. This argued that the major form of SOS regulation is by its redistribution from the cytoplasm to the EGF receptor and presumably into the vicinity of its target Ras.
-
(1993)
Cell
, vol.73
, pp. 611-620
-
-
Buday1
Downward2
-
45
-
-
0027304731
-
Human Sos-1: A Guanine Nucleotide Exchange Factor for Ras that Binds to GRB2
-
of special interest, With [16,44⊎,46⊎–48⊎], shows that the activation of the EGF receptor leads to complex formation between the receptor, the adaptor protein, Grb2, and the Ras activator, mSOS. This paper was unique in that it showed for the first time that SOS can actually promote nucleotide exchange of Ras in vitro.
-
(1993)
Science
, vol.260
, pp. 1338-1343
-
-
Chardin1
Camonis2
Gale3
Van Aelst4
Schlessinger5
Wigler6
Bar-Sagi7
-
46
-
-
0027910431
-
Association of SOS Ras Exchange Protein with GRB2 is Implicated in Tyrosine Kinase Signal Transduction and Transformation
-
of special interest, Along with [16,44⊎,45⊎,47⊎,48⊎], shows that the activation of the EGF receptor leads to complex formation between the receptor, the adaptor protein, Grb2, and the Ras activator, mSOS. This paper made extensive use of epitope-tagged signalling molecules. This allowed the proteins to be studied upon transfection into tissue culture cells, without having to make specific antibodies to each signalling molecule.
-
(1993)
Nature
, vol.363
, pp. 45-50
-
-
Egan1
Giddings2
Brooks3
Buday4
Sizeland5
Weinberg6
-
47
-
-
0027312272
-
Guanine-Nucleotide-Releasing Factor hSOS Binds to Grb2 and Linkss Receptor Tyrosine Kinases to Ras Signalling
-
of special interest, One of six papers [16,44⊎–46⊎,48⊎] that came out at the same time showing that the activation of the EGF receptor leads to complex formation between the receptor, the adaptor protein, Grb2, and the Ras activator, mSOS.
-
(1993)
Nature
, vol.363
, pp. 85-88
-
-
Li1
Batzer2
Daly3
Yajnik4
Skolnick5
Chardin6
Bar-Sagi7
Margolis8
Schlessinger9
-
48
-
-
0027324057
-
Molecular Cloning of the Mouse grb2 Gene: Differential Interaction of the Grb2 Adaptor Protein with Epidermal Growth Factor and Nerve Growth Factor Receptors
-
of special interest, Grb2 is not found complexed to the TrkA nerve growth factor receptor, despite the fact that nerve growth factor treatment of cells leads to Ras activation. Like the insulin system, it is possible that Grb2 or some other adaptor molecule binds to a substrate of TrkA, instead of to the receptor itself. This would create a docking site for the Ras exchange factor SOS.
-
(1993)
Mol Cell Biol
, vol.13
, pp. 5500-5512
-
-
Suen1
Bustelo2
Pawson3
Barbacid4
-
51
-
-
0027411213
-
Pertussis Toxin-Sensitive Activation of P21ras by G Protein-Coupled Receptor Agonists in Fibroblasts
-
i,o class. Ligands used were lysophosphatidic acid and thrombin. This pathway was blocked by tyrosine kinase inhibitors, suggesting a connection with the Grb2-SOS proteins.
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 1257-1261
-
-
Van Corven1
Hordijk2
Medema3
Bos4
Moolenaar5
-
53
-
-
0027240231
-
i-Coupled Acetylcholine Muscarinic m2 Receptor Activation of Mitogen-Activated Protein (MAP) Kinase Kinase and MAP Kinase
-
i. This response is not blocked by the tyrosine kinase inhibitors, suggesting a novel non-Grb2-SOS pathway to Ras.
-
(1993)
J Biol Chem
, vol.268
, pp. 19196-19199
-
-
Winitz1
Russell2
Qian3
Garner4
Dwyer5
Johnson6
-
55
-
-
0026768072
-
Isolation of Multiple Mouse cDNAs with Coding Homology to Saccharomyces cerevisiae CDC25: Identification of a Region Related to Bcr, Vav, Dbl and CDC24
-
Mm; same as Ras-GRF, [28⊎]. It revealed that in addition to a Ras-activating domain at the carboxyl terminus, a Dbl-like domain exists near the amino terminus that may encode a GEF activity for a second member of the Ras superfamily. Preliminary data suggested that smaller forms of the 140kDa full-length protein are expressed in some cells.
-
(1992)
EMBO J
, vol.11
, pp. 4007-4015
-
-
Cen1
Papageorge2
Zippel3
Lowy4
Zhang5
-
61
-
-
0026632813
-
Mutations of Ha-Ras p21 that Define Important Regions for the Molecular Mechanism of the SDC25 C-Domain, a Guanine Nucleotide Dissociation Stimulator
-
of special interest, This paper analyzed a wide number of Ras mutants for their interaction with a yeast exchange factor, SDC25. Mutations in both regions of Ras that change conformation upon GTP binding suppressed responsiveness to SDC25. However, the mutants did not suppress binding of Ras to the exchange factor, suggesting these sites are required for inducing nucleotide release, but are not directly involved in binding exchange factors.
-
(1992)
EMBO J
, vol.11
, pp. 2391-2397
-
-
Mitsou1
Jacquet2
Poullet3
Rensland4
Gidion5
Schlichtling6
Wittinghofer7
Parmeggiani8
-
63
-
-
0022238094
-
A Study of the Kinetic Mechanism of Elongation Factor Ts
-
(1985)
J Biol Chem
, vol.260
, pp. 11498-11502
-
-
Hwang1
Miller2
-
64
-
-
0027502176
-
Influence of Guanine Nucleotides on Complex Formation Between Ras and CDC25 Proteins
-
of special interest, This paper shows that nucleotide-free Ras binds very tightly to exchange factors.
-
(1993)
Mol Cell Biol
, vol.13
, pp. 1345-1352
-
-
Lai1
Boguski2
Broek3
Powers4
-
65
-
-
0024599698
-
Dominant Yeast and Mammalian Ras Mutants that Interfere with the CDC25-Dependent Activation of Wild-Type RAS in Saccharomyces cerevisiae
-
(1989)
Mol Cell Biol
, vol.9
, pp. 390-395
-
-
Powers1
Wigler2
-
67
-
-
0026628881
-
RAS Residues that are Distant from the GDP Binding Site Play a Critical Role in Dissociation Factor-Stimulated Release of GDP
-
of special interest, Mutations around Ras amino acid 73 (in the mammalian H-Ras sequence) blocked GEF effects on Ras without altering intrinsic interactions of Ras with nucleotides. This region may be involved in GEF binding; however, it is highly conserved in other Ras family members that have their own GEFs. This implies that other sites are involved in binding specificity. Interestingly, the widely used 259 anti-Ras monoclonal antibody binds to this region of Ras and is known to inhibit nucleotide exchange.
-
(1992)
EMBO J
, vol.11
, pp. 2855-2862
-
-
Verotti1
Crechet2
Di Blasi3
Seidita4
Mirisola5
Kavounis6
Nastopoulos7
Burderi8
De Vendittis9
Parmeggiani10
Fasano11
-
68
-
-
0027175224
-
Residues Crucial for Ras Interaction with GDP-GTP Exchangers
-
of special interest, Mutations in Ras around amino acids 105–108 block effects of exchange factors in yeast. This alteration does not block oncogenic Ras from stimulating downstream targets in yeast. Thus, this region may be involved in binding exchange factors.
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 5564-5568
-
-
Segal1
Willumsen2
Levitzki3
-
69
-
-
0026463861
-
Amino Acid Residues in the Ras-Like GTPase Rab3A that Specify Sensitivity to Factors that Regulate the GTP/GDP Cycling of Rab3A
-
(1992)
J Biol Chem
, vol.267
, pp. 22715-22718
-
-
Burstein1
Brondyk2
Macara3
-
70
-
-
0027158878
-
Mutants of Rab3A Analogous to Oncogenic Ras Mutants-Sensitivity to Rab3A-GTPase Activating Protein and Rab3A-Guanine Nucleotide Releasing Factor
-
(1993)
J Biol Chem
, vol.268
, pp. 9410-9415
-
-
Brondyk1
Mckiernan2
Burstein3
Macara4
|