Search results for "GRB2"

showing 2 items of 2 documents

Requirement of caveolae microdomains in extracellular signal-regulated kinase and focal adhesion kinase activation induced by endothelin-1 in primary…

1999

Endothelin-1 (ET-1) mitogenic activity in astrocytes is mediated by the activation of the extracellular signal-regulated kinase (ERK) pathway together with the Rho-dependent activation of the focal adhesion kinase (FAK) pathway. To clarify the mechanisms responsible for the coordinate activation of both pathways in the ET-1 signal propagation, the involvement of caveolae microdomains, suggested to play a role in signal transduction, was evaluated. In this study, it is reported that caveolae of primary astrocytes are enriched in endothelin receptor (ETB-R). Furthermore, signaling molecules such as the adaptor proteins Shc and Grb2, and the small G protein Rho, also reside within these microd…

MAPK/ERK pathwayCaveolin 1BiologyBiochemistryCaveolinsFocal adhesionCellular and Molecular Neurosciencechemistry.chemical_compoundCaveolaeCell AdhesionAnimalsFilipinPhosphorylationCells CulturedCytoskeletonMitogen-Activated Protein Kinase 1Endothelin-1Signal transducing adaptor proteinMembrane ProteinsTyrosine phosphorylationProtein-Tyrosine KinasesActinsCell biologyAnti-Bacterial AgentsCell CompartmentationRatsEnzyme ActivationchemistryAstrocytesFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesCaveolin 1Calcium-Calmodulin-Dependent Protein Kinasesbiology.proteinTyrosineGRB2Signal transductionExtracellular SpaceCell Adhesion MoleculesSignal TransductionJournal of neurochemistry
researchProduct

Plasticity of the PAS domain and a potential role for signal transduction in the histidine kinase DcuS

2008

The mechanistic understanding of how membrane-embedded sensor kinases recognize signals and regulate kinase activity is currently limited. Here we report structure-function relationships of the multidomain membrane sensor kinase DcuS using solid-state NMR, structural modeling and mutagenesis. Experimental data of an individual cytoplasmic Per-Arnt-Sim (PAS) domain were compared to structural models generated in silico. These studies, together with previous NMR work on the periplasmic PAS domain, enabled structural investigations of a membrane-embedded 40-kDa construct by solid-state NMR, comprising both PAS segments and the membrane domain. Structural alterations are largely limited to prot…

Models MolecularCytoplasmHistidine KinaseMolecular Sequence DataHAMP domainStructural BiologyPAS domainEscherichia coliAmino Acid SequenceKinase activityProtein Structure QuaternaryNuclear Magnetic Resonance BiomolecularMolecular BiologybiologyEscherichia coli ProteinsHistidine kinaseProtein Structure TertiaryCell biologyTransmembrane domainBiochemistryProtein kinase domainCyclic nucleotide-binding domainbiology.proteinGRB2Protein KinasesSignal Transduction
researchProduct