Search results for "GTP Phosphohydrolases"

showing 3 items of 23 documents

Ras, Rap, and Rac Small GTP-binding Proteins Are Targets for Clostridium sordellii Lethal Toxin Glucosylation

1996

Lethal toxin (LT) from Clostridium sordellii is one of the high molecular mass clostridial cytotoxins. On cultured cells, it causes a rounding of cell bodies and a disruption of actin stress fibers. We demonstrate that LT is a glucosyltransferase that uses UDP-Glc as a cofactor to covalently modify 21-kDa proteins both in vitro and in vivo. LT glucosylates Ras, Rap, and Rac. In Ras, threonine at position 35 was identified as the target amino acid glucosylated by LT. Other related members of the Ras GTPase superfamily, including RhoA, Cdc42, and Rab6, were not modified by LT. Incubation of serum-starved Swiss 3T3 cells with LT prevents the epidermal growth factor-induced phosphorylation of m…

ThreonineUridine Diphosphate GlucoseRHOABacterial ToxinsMolecular Sequence DataClostridium sordelliimacromolecular substancesCDC42GTPaseBiologyCell morphologyBiochemistryGTP PhosphohydrolasesProto-Oncogene Proteins p21(ras)MiceGTP-binding protein regulatorsGTP-Binding ProteinsAnimalsHumansAmino Acid SequenceMolecular BiologyClostridiumEpidermal Growth FactorKinase3T3 CellsCell Biologybiology.organism_classificationMolecular biologyActinsrac GTP-Binding ProteinsActin CytoskeletonKineticsGlucoserap GTP-Binding ProteinsGlucosyltransferasesCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinPhosphorylationGuanosine TriphosphateHeLa CellsJournal of Biological Chemistry
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rhoB encoding a UV-inducible Ras-related small GTP-binding protein is regulated by GTPases of the Rho family and independent of JNK, ERK, and p38 MAP…

1998

The small GTPase RhoB is immediate-early inducible by DNA damaging treatments and thus part of the early response of eukaryotic cells to genotoxic stress. To investigate the regulation of this cellular response, we isolated the gene for rhoB from a mouse genomic library. Sequence analysis of the rhoB gene showed that its coding region does not contain introns. The promoter region of rhoB harbors regulatory elements such as TATA, CAAT, and Sp1 boxes but not consensus sequences for AP-1, Elk-1, or c-Jun/ATF-2. The rhoB promoter was activated by UV irradiation, but not by 12-O-tetradecanoylphorbol-13-acetate treatment. rhoB promoter deletion constructs revealed a fragment of 0.17 kilobases in …

Ultraviolet RaysRHOBMolecular Sequence DataMAP Kinase Kinase Kinase 1BiologyProtein Serine-Threonine KinasesBiochemistryp38 Mitogen-Activated Protein KinasesGTP PhosphohydrolasesWortmanninchemistry.chemical_compoundMiceGTP-Binding ProteinsRhoB GTP-Binding ProteinAnimalsCloning MolecularEnzyme InhibitorsPromoter Regions GeneticrhoB GTP-Binding ProteinMolecular BiologyPhosphoinositide-3 Kinase InhibitorsMAP kinase kinase kinaseBase SequenceKinaseMEK inhibitorJNK Mitogen-Activated Protein KinasesMembrane ProteinsCell BiologyMolecular biologychemistryMitogen-activated protein kinaseCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinras ProteinsSignal transductionMitogen-Activated Protein KinasesThe Journal of biological chemistry
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Rho GTPases are over-expressed in human tumors.

1999

Small GTPases of the Rho family are involved in the regulation of a variety of cellular processes, such as the organization of the microfilamental network, cell-cell contact and malignant transformation. To address the question of whether Rho proteins are involved in carcinogenesis in man, we compared their expression in tumors from colon, breast and lung with that of the corresponding normal tissue originating from the same patient. As shown by Rho-specific 32P-ADP-ribosylation, as well as Western-blot analysis, the amount of RhoA protein was largely increased in all 3 types of tumors tested. The most dramatic differences in the expression of Rho GTPases were observed in breast tissue. All…

rho GTP-Binding ProteinsCancer ResearchPathologymedicine.medical_specialtyRHOALung NeoplasmsColonBreast NeoplasmsCell Cycle ProteinsGTPaseCDC42medicine.disease_causeMalignant transformationGTP PhosphohydrolasesGTP-Binding ProteinsmedicineHumansrho-Specific Guanine Nucleotide Dissociation InhibitorsBreastcdc42 GTP-Binding ProteinrhoB GTP-Binding ProteinLungGuanine Nucleotide Dissociation InhibitorsMitogen-Activated Protein Kinase 1Adenosine Diphosphate RibosebiologyCancerMembrane Proteinsmedicine.diseaseImmunohistochemistryrac GTP-Binding ProteinsOncologyrhoC GTP-Binding ProteinCalcium-Calmodulin-Dependent Protein KinasesColonic Neoplasmsbiology.proteinCancer researchImmunohistochemistryCarcinogenesisrhoA GTP-Binding ProteinRhoC GTP-Binding ProteinInternational journal of cancer
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