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  • 1
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    Early enhancement of calcium currents by H-ras oncoproteins injected into Hermissenda neurons (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-12-21
    Description: Influx of calcium through membrane channels is an important initial step in signal transduction of growth signals. Therefore, the effects of Ras protein injection on calcium currents across the soma membrane of an identified neuron of the snail Hermissenda were examined. With the use of these post-mitotic cells, a voltage-sensitive, inward calcium current was increased 10 to 20 minutes after Harvey-ras oncoproteins were injected. The effects of oncogenic Harvey ras p21 protein (v-Ras) occurred quickly and were sustained, whereas the effects of proto-oncogenic ras protein (c-Ras) were transient. This relative potency is consistent with the activities of these oncoproteins in stimulating cell proliferation. Thus, this calcium channel may be a target for Ras action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Collin, C -- Papageorge, A G -- Lowy, D R -- Alkon, D L -- New York, N.Y. -- Science. 1990 Dec 21;250(4988):1743-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular and Cellular Neurobiology, NINDS-NIH, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2176747" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Barium/pharmacology ; Calcium Channels/drug effects/*physiology ; In Vitro Techniques ; Membrane Potentials/drug effects ; Microinjections ; Neurons/*physiology ; Oncogene Protein p21(ras)/administration & dosage/*pharmacology ; Potassium Channels/drug effects/physiology ; Proto-Oncogene Proteins p21(ras)/administration & dosage/*pharmacology ; Snails
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Mechanistic aspects of signaling through Ras in NIH 3T3 cells (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-31
    Description: Serum and growth factors can increase the proportion of Ras in the active guanosine triphosphate (GTP)-bound form. Growth factors might stimulate guanine nucleotide exchange or decrease the activity of the guanosine triphosphatase-activating proteins GAP and neurofibromin (NF1). In NIH 3T3 cells that overexpress the mutant Ras protein His116, which releases bound guanine nucleotide at a constitutively high rate and retains sensitivity to GAP and NF1, the proportion of GTP bound to the His116 protein was not altered by serum or platelet-derived growth factor. However, these mitogens increased the proportion of Ras in the GTP-bound form in cells that overexpressed control Ras proteins with a normal intrinsic rate of guanine nucleotide release. The amount of GTP-bound His116 or control Ras proteins was higher in cells at low density than in cells at high density, which have more GAP-like activity. The lower proportion of GTP-bound Ras in NIH 3T3 cells at high density may result from increased GAP-like activity. By contrast, serum and platelet-derived growth factors appear to stimulate guanine nucleotide exchange.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, K -- Papageorge, A G -- Lowy, D R -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):671-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular Oncology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496380" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Blood ; Cell Line, Transformed ; Fibroblasts/*metabolism ; GTPase-Activating Proteins ; Gene Expression ; Genes, ras/*physiology ; Growth Substances/*pharmacology ; Guanosine Triphosphate/*metabolism ; Histidine ; Methionine ; Mice ; Mutagenesis ; Neurofibromin 1 ; Platelet-Derived Growth Factor/pharmacology ; Proteins/pharmacology ; Proto-Oncogene Proteins p21(ras)/chemistry/genetics/*metabolism ; Signal Transduction/*genetics ; ras GTPase-Activating Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Identification of small clusters of divergent amino acids that mediate the opposing effects of ras and Krev-1 (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-07-13
    Description: Krev-1 is an anti-oncogene that was originally identified by its ability to induce morphologic reversion of ras-transformed cells that continue to express the ras gene. The Krev-1-encoded protein is structurally related to Ras proteins. The biological activities of a series of ras-Krev-1 chimeras were studied to test the hypothesis that Krev-1 may directly interfere with a ras function. The ras-specific and Krev-1-specific amino acids immediately surrounding residues 32 to 44, which are identical between the two proteins, determined whether the protein induced cellular transformation or suppressed ras transformation. Because this region in Ras proteins has been implicated in effector function, the results suggest that Krev-1 suppresses ras-induced transformation by interfering with interaction of Ras with its effector.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, K -- Noda, M -- Vass, W C -- Papageorge, A G -- Lowy, D R -- New York, N.Y. -- Science. 1990 Jul 13;249(4965):162-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular Oncology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2115210" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/*physiology ; Animals ; Cell Transformation, Neoplastic/*genetics ; Chimera ; GTP-Binding Proteins/*genetics ; *Gene Expression Regulation, Neoplastic ; *Genes, ras ; Harvey murine sarcoma virus/genetics ; Molecular Sequence Data ; Mutation ; Restriction Mapping ; *Suppression, Genetic ; rap GTP-Binding Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Heterogeneous amino acids in Ras and Rap1A specifying sensitivity to GAP proteins (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-13
    Description: Guanosine triphosphatase (GTPase) activity of Ras is increased by interaction with Ras-GAP (GTPase-activating protein) or with the GAP-related domain of the type 1 neurofibromatosis protein (NF1-GRD), but Ras is not affected by interaction with cytoplasmic and membrane forms of Rap-GAP; Rap1A, whose effector function can suppress transformation by Ras, is sensitive to both forms of Rap-GAP and resistant to Ras-GAP and NF1-GRD. A series of chimeric proteins composed of portions of Ras and Rap were constructed; some were sensitive to Ras-GAP but resistant to NF1-GRD, and others were sensitive to cytoplasmic Rap-GAP but resistant to membrane Rap-GAP. Sensitivity of chimeras to Ras-GAP and cytoplasmic Rap-GAP was mediated by amino acids that are carboxyl-terminal to the effector region. Residues 61 to 65 of Ras conferred Ras-GAP sensitivity, but a larger number of Rap1A residues were required for sensitivity to cytoplasmic Rap-GAP. Chimeras carrying the Ras effector region that were sensitive only to Ras-GAP or only to cytoplasmic Rap-GAP transformed NIH 3T3 cells poorly. Thus, distinct amino acids of Ras and Rap1A mediate sensitivity to each of the proteins with GAP activity, and transforming potential of Ras and sensitivity of Ras to Ras-GAP are at least partially independent properties.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, K -- Papageorge, A G -- Martin, P -- Vass, W C -- Olah, Z -- Polakis, P G -- McCormick, F -- Lowy, D R -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1630-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular Oncology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1749934" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/metabolism ; Cytosol/metabolism ; Enzyme Activation ; GTP-Binding Proteins/*physiology ; GTPase-Activating Proteins ; Genes, Neurofibromatosis 1 ; In Vitro Techniques ; Proteins/*physiology ; Proto-Oncogene Proteins p21(ras)/*physiology ; Recombinant Fusion Proteins ; Structure-Activity Relationship ; rap GTP-Binding Proteins ; ras GTPase-Activating Proteins
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Transfection of v-rasH DNA into MCF-7 human breast cancer cells bypasses dependence on estrogen for tumorigenicity (1985)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1985-05-10
    Description: The natural history of estrogen-responsive breast cancers often involves a phenotypic change to an estrogen-unresponsive, more aggressive tumor. The human breast cancer cell line, MCF-7, which requires estradiol for tumor formation in vivo and shows growth stimulation in response to estradiol in vitro, is a model for hormone-responsive tumors. The v-rasH onc gene was transfected into MCF-7 cells. The cloned MCF-7ras transfectants, which expressed the v-rasH messenger RNA and v-rasH p21 protein (21,000 daltons), were characterized. In contrast to the parental cell line, MCF-7ras cells no longer responded to exogenous estrogen in culture and their growth was minimally inhibited by exogenous antiestrogens. When tested in the nude mouse, the MCF-7ras cells were fully tumorigenic in the absence of estrogen supplementation. Thus, cells acquiring an activated onc gene can bypass the hormonal regulatory signals that trigger the neoplastic growth of a human breast cancer cell line.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kasid, A -- Lippman, M E -- Papageorge, A G -- Lowy, D R -- Gelmann, E P -- New York, N.Y. -- Science. 1985 May 10;228(4700):725-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/4039465" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breast Neoplasms/chemically induced/*genetics ; Cell Line ; Cell Transformation, Neoplastic/*chemically induced ; DNA, Neoplasm/genetics ; Estrogens/*pharmacology ; Female ; Humans ; Mice ; Mice, Nude ; Neoplasms, Experimental/chemically induced/genetics ; *Oncogenes ; Pyrrolidines/pharmacology ; Repetitive Sequences, Nucleic Acid ; Thiophenes/pharmacology ; *Transfection
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Guanine nucleotide-binding activity as an assay for src protein of rat-derived murine sarcoma viruses (1979)
    National Academy of Sciences
    Details
    Publication Date: 1979-10-01
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 7
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    Oncogenic inhibition by a deleted in liver cancer gene requires cooperation between tensin binding and Rho-specific GTPase-activating protein activities (2007)
    National Academy of Sciences
    Details
    Publication Date: 2007-05-15
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 8
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    Full activity of the deleted in liver cancer 1 (DLC1) tumor suppressor depends on an LD-like motif that binds talin and focal adhesion kinase (FAK) (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-10-03
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 9
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    Full activity of the deleted in liver cancer 1 (DLC1) tumor suppressor depends on an LD-like motif that binds talin and focal adhesion kinase (FAK) [Medical Sciences] (2011)
    National Academy of Sciences
    Details
    Publication Date: 2011-10-12
    Description: The deleted in liver cancer 1 (DLC1) tumor suppressor gene, which is frequently inactivated in cancer, encodes a Rho-GAP (GTPase activating protein) focal adhesion protein whose negative regulation of Rho-GTPases is necessary but not sufficient for its full tumor suppressor activity. Here, we report that DLC1 forms a complex with two prooncogenic focal adhesion proteins, talin and the focal adhesion kinase (FAK). We identified an 8-aa sequence (residues 469LDDILYHV476) in DLC1 and designated it an LD-like motif, because it shares homology with the LD motifs of paxillin. This motif was necessary for DLC1 binding to talin and FAK, because a DLC1 mutant, from which six of the residues have been deleted, and another mutant carrying amino acid substitutions in three of the residues are deficient for binding both proteins and localization of DLC1 to focal adhesions. FAK binding was independent of talin and vice versa. In bioassays, both DLC1 mutants were less active than wild-type (WT) DLC1, although the ability of the mutants to negatively regulate overall Rho-GTP was not impaired. We conclude that the LD-like motif, which binds talin and FAK, is required for the full tumor suppressor activity of DLC1 and contributes to the association of DLC1 with focal adhesions.
    Print ISSN: 0027-8424
    Electronic ISSN: 1091-6490
    Topics: Biology , Medicine , Natural Sciences in General
    Published by National Academy of Sciences
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  • 10
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    RIT1 oncoproteins escape LZTR1-mediated proteolysis (2019)
    American Association for the Advancement of Science (AAAS)
    In: Science
    Details
    Publication Date: 2019
    Description: 〈p〉RIT1 oncoproteins have emerged as an etiologic factor in Noonan syndrome and cancer. Despite the resemblance of RIT1 to other members of the Ras small guanosine triphosphatases (GTPases), mutations affecting RIT1 are not found in the classic hotspots but rather in a region near the switch II domain of the protein. We used an isogenic germline knock-in mouse model to study the effects of RIT1 mutation at the organismal level, which resulted in a phenotype resembling Noonan syndrome. By mass spectrometry, we detected a RIT1 interactor, leucine zipper–like transcription regulator 1 (LZTR1), that acts as an adaptor for protein degradation. Pathogenic mutations affecting either RIT1 or LZTR1 resulted in incomplete degradation of RIT1. This led to RIT1 accumulation and dysregulated growth factor signaling responses. Our results highlight a mechanism of pathogenesis that relies on impaired protein degradation of the Ras GTPase RIT1.〈/p〉
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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