Matches in Nanopublications for { ?s ?p "LSC (also known as ARHGEF1) is a haematopoietic cell-restricted GEF for RHOA, which interacts with G protein-coupled receptor (GPCR)-associated Galpha12 and Galpha13 proteins (Fig. 5). In addition to its DH domain with GEF activity, LSC has a regulator of G protein signalling (RGS) domain, which binds to Galpha proteins and increases their intrinsic GTPase activity, thereby turning off GPCR signalling. So LSC seems to carry out two functions. First, it transduces GPCR signals from Galpha12 and Galpha13 proteins to activate RHOA and second, it attenuates other Galpha12- or Galpha13-coupled GPCR signals. In LSC-deficient mice, the number of B cells is decreased as are T cell-dependent antibody responses to protein antigens owing to a cell-intrinsic requirement for LSC in B cells27, 28. Further analysis has shown that LSC-deficient marginal zone B cells migrate more effectively in response to sphingosine 1-phosphate (S1P) in vitro, which might be due to the loss of LSC-mediated inhibition of signalling from Galpha12/13-coupled S1P receptors. By contrast, LSC-deficient marginal zone B cells have a defect in their ability to detach from ICAM1 and they do not migrate to the follicles following LPS stimulation in vivo. The defects in migration to the follicles might reflect a requirement for LSC-mediated RHOA activation in the disengagement of integrin binding at the trailing edge of the migrating B cell28. " ?g. }
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- _6 value "LSC (also known as ARHGEF1) is a haematopoietic cell-restricted GEF for RHOA, which interacts with G protein-coupled receptor (GPCR)-associated Galpha12 and Galpha13 proteins (Fig. 5). In addition to its DH domain with GEF activity, LSC has a regulator of G protein signalling (RGS) domain, which binds to Galpha proteins and increases their intrinsic GTPase activity, thereby turning off GPCR signalling. So LSC seems to carry out two functions. First, it transduces GPCR signals from Galpha12 and Galpha13 proteins to activate RHOA and second, it attenuates other Galpha12- or Galpha13-coupled GPCR signals. In LSC-deficient mice, the number of B cells is decreased as are T cell-dependent antibody responses to protein antigens owing to a cell-intrinsic requirement for LSC in B cells27, 28. Further analysis has shown that LSC-deficient marginal zone B cells migrate more effectively in response to sphingosine 1-phosphate (S1P) in vitro, which might be due to the loss of LSC-mediated inhibition of signalling from Galpha12/13-coupled S1P receptors. By contrast, LSC-deficient marginal zone B cells have a defect in their ability to detach from ICAM1 and they do not migrate to the follicles following LPS stimulation in vivo. The defects in migration to the follicles might reflect a requirement for LSC-mediated RHOA activation in the disengagement of integrin binding at the trailing edge of the migrating B cell28. " provenance.
- _6 value "LSC (also known as ARHGEF1) is a haematopoietic cell-restricted GEF for RHOA, which interacts with G protein-coupled receptor (GPCR)-associated Galpha12 and Galpha13 proteins (Fig. 5). In addition to its DH domain with GEF activity, LSC has a regulator of G protein signalling (RGS) domain, which binds to Galpha proteins and increases their intrinsic GTPase activity, thereby turning off GPCR signalling. So LSC seems to carry out two functions. First, it transduces GPCR signals from Galpha12 and Galpha13 proteins to activate RHOA and second, it attenuates other Galpha12- or Galpha13-coupled GPCR signals. In LSC-deficient mice, the number of B cells is decreased as are T cell-dependent antibody responses to protein antigens owing to a cell-intrinsic requirement for LSC in B cells27, 28. Further analysis has shown that LSC-deficient marginal zone B cells migrate more effectively in response to sphingosine 1-phosphate (S1P) in vitro, which might be due to the loss of LSC-mediated inhibition of signalling from Galpha12/13-coupled S1P receptors. By contrast, LSC-deficient marginal zone B cells have a defect in their ability to detach from ICAM1 and they do not migrate to the follicles following LPS stimulation in vivo. The defects in migration to the follicles might reflect a requirement for LSC-mediated RHOA activation in the disengagement of integrin binding at the trailing edge of the migrating B cell28. " provenance.