Search results for "Pleckstrin homology domain"

showing 3 items of 3 documents

Binding properties and stability of the Ras-association domain of Rap1-GTP interacting adapter molecule (RIAM).

2012

The Rap1-GTP interacting adapter protein (RIAM) is an important protein in Rap1-mediated integrin activation. By binding to both Rap1 GTPase and talin, RIAM recruits talin to the cell membrane, thus facilitating talin-dependent integrin activation. In this article, we studied the role of the RIAM Ras-association (RA) and pleckstrin-homology (PH) domains in the interaction with Rap1. We found that the RA domain was sufficient for GTP-dependent interaction with Rap1B, and the addition of the PH domain did not change the binding affinity. We also detected GTP-independent interaction of Rap1B with the N-terminus of RIAM. In addition, we found that the PH domain stabilized the RA domain both in …

TalinIntegrinsGTP'lcsh:MedicineGTPaseSignal transductionBiochemistryProtein structureMolecular cell biologyRIAMlcsh:Science0303 health sciencesMultidisciplinarybiologyProtein Stability030302 biochemistry & molecular biologySignal transducing adaptor proteinrap1 GTP-Binding ProteinssitoutuminenCell biologyPleckstrin homology domainRap1Research Articleendocrine systemvuorovaikutusProtein domainIntegrinSignaling in cellular processesPhosphoinositide Signal TransductionSignaling Pathways03 medical and health sciencesCell AdhesionHumansProtein InteractionsBiologyGTPase signaling030304 developmental biologyRas signalingAdaptor Proteins Signal Transducingintegriinitlcsh:RProteinsMembrane ProteinsRegulatory ProteinsProtein Structure TertiaryCytoskeletal Proteinsenzymes and coenzymes (carbohydrates)rap GTP-Binding ProteinsCell movement signalingbiology.proteinta1181lcsh:QPLoS ONE
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The estrogen receptor α:insulin receptor substrate 1 complex in breast cancer: structure–function relationships

2007

Background: Insulin receptor substrate 1 (IRS-1) is a signaling molecule that exerts a key role in mediating cross talk between estrogen receptor a (ERa) and insulin-like growth factor 1 (IGF-1) in breast cancer cells. Previously, we demonstrated that a fraction of IRS-1 binds ERa, translocates to the nucleus, and modulates ERa-dependent transcription at estrogen response elements (ERE). Here, we studied structure-function relationships of the ER-a:IRS-1 complex under IGF-1 and/or estradiol (E 2 ) stimulation. Materials and methods: ERa and IRS-1 deletion mutants were used to analyze structural and functional ERα/IRS-1 interactions. IRS-1 binding to ERE and IRS-1 role in ERa-dependent ERE t…

medicine.medical_specialtyInsulin Receptor Substrate ProteinsActive Transport Cell NucleusEstrogen receptorRepressorBreast NeoplasmsBiologyStructure-Activity Relationshipestrogen receptor alpha (ERa) Insulin receptor substrate 1 (IRS-1) breast cancerCell Line TumorInternal medicineCoactivatormedicineHumansInsulin-Like Growth Factor IReceptors InterferonEstradiolEstrogen Receptor alphaHematologyDNA-binding domainPhosphoproteinsPeptide FragmentsReceptor InsulinProtein Structure TertiaryCell biologyIRS1Repressor ProteinsPleckstrin homology domainEndocrinologyOncologyInsulin Receptor Substrate ProteinsFemaleChromatin immunoprecipitationProtein BindingAnnals of Oncology
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PLEKHM1 Regulates Salmonella-Containing Vacuole Biogenesis and Infection

2015

Abstract: The host endolysosomal compartment is often manipulated by intracellular bacterial pathogens. Salmonella (Salmonella enterica serovar Typhimurium) secrete numerous effector proteins, including SifA, through a specialized type III secretion system to hijack the host endosomal system and generate the Salmonella-containing vacuole (SCV). To form this replicative niche, Salmonella targets the Rab7 GTPase to recruit host membranes through largely unknown mechanisms. We show that Pleckstrin homology domain-containing protein family member 1 (PLEKHM1), a lysosomal adaptor, is targeted by Salmonella through direct interaction with SifA. By binding the PLEKHM1 PH2 domain, Salmonella utiliz…

SalmonellaCancer ResearchbiologyEffectorEndosomeVacuolebiology.organism_classificationmedicine.disease_causeMicrobiologyType three secretion systemMicrobiologyPleckstrin homology domainSalmonella entericaVirologyImmunology and Microbiology(all)medicineParasitologySecretionHuman medicineBiologyMolecular BiologyCell Host & Microbe
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