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Signaling Responses of B Lymphocytes
*
B Cell Molecular Immunology Section, Laboratory of Immunoregulation, and
Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892; and
Department of Pharmacology, University of Texas Southwestern Medical Center, Dallas, TX 75235
Regulator of G protein signaling (RGS) proteins modulate signaling
through pathways that use heterotrimeric G proteins as transducing
elements. RGS1 is expressed at high levels in certain B cell lines and
can be induced in normal B cells by treatment with TNF-
. To
determine the signaling pathways that RGS1 may regulate, we examined
the specificity of RGS1 for various G subunits and
assessed its effect on chemokine signaling. G protein binding and
GTPase assays revealed that RGS1 is a Gi and
Gq GTPase-activating protein and a potential
G12 effector antagonist. Functional studies
demonstrated that RGS1 impairs platelet activating factor-mediated
increases in intracellular Ca+2, stromal-derived
factor-1-induced cell migration, and the induction of downstream
signaling by a constitutively active form of
G12. Furthermore, germinal center B
lymphocytes, which are refractory to stromal-derived factor-1-triggered
migration, express high levels of RGS1. These results indicate that RGS
proteins can profoundly effect the directed migration of lymphoid
cells.
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