![[Feedback]](/icons/banner/feedbackACT.gif){kind=icon}
![[For Subscribers]](/icons/banner/subscriberACT.gif){kind=icon}
![[Archive]](/icons/banner/archiveACT.gif){kind=icon}
![[Search]](/icons/banner/searchACT.gif){kind=icon}
![[Contents]](/icons/banner/tocACT.gif){kind=icon}
|
|
|
|
|
||
Vol. 58, Issue 3, 569-576, September 2000
, Attenuates Gi-
and G13-Mediated Signaling Pathways
B-Cell Molecular Immunology Section, Laboratory of
Immunoregulation, National Institute of Allergy and Infectious
Diseases, National Institutes of Health, Bethesda, Maryland (H.C.,
K.T., J.H.K.); Section de Recherche, Institut Curie, Paris, France
(J.D.G.); and Department of Pharmacology, University of Illinois,
Chicago, Illinois (T.K.)
Regulator of G protein signaling (RGS) proteins are a family of
approximately 20 proteins that negatively regulate signaling through
heterotrimeric G protein-coupled receptors. The RGS proteins act as
GTPase-activating proteins (GAPs) for certain G
subunits and as
effector antagonists for Gq. Mouse RGS14 encodes a
547-amino-acid protein with an N-terminal RGS domain, which is highly
expressed in lymphoid tissues. In this study, we demonstrate that RGS14 is a GAP for Gi subfamily members and it attenuates interleukin-8 receptor-mediated mitogen-activated protein kinase activation. However, RGS14 does not exhibit GAP activity toward Gs or Gq nor
does it regulate Gs- or Gq-mediated signaling pathways. Although
RGS14 does not act as a GAP for G12/13, it impairs
c-fos serum response element activation induced by
either a constitutively active mutant of G13 (G13Q226L) or by
carbachol stimulation of muscarinic type 1 receptors. An RGS14 mutant
(EN92/93AA), which does not block Gi-linked signaling, also inhibits
serum response element activation. RGS14 localizes predominantly in the
cytosol, but it can be recruited to membranes by expression of
G13Q226L. Although RGS14 is constitutively expressed in lymphoid
cells, agents that activate B or T lymphocytes further enhance its
levels. Taken together, our results suggest that signals generated
after lymphocyte activation may via RGS14 directly impinge on Gi- or G13-mediated cellular processes in lymphocytes, such as adhesion and migration.
This article has been cited by other articles:
|
|
 |
|
  M. Soundararajan, F. S. Willard, A. J. Kimple, A. P. Turnbull, L. J. Ball, G. A. Schoch, C. Gileadi, O. Y. Fedorov, E. F. Dowler, V. A. Higman, et al. Structural diversity in the RGS domain and its interaction with heterotrimeric G protein {alpha}-subunits PNAS, April 29, 2008; 105(17): 6457 - 6462. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Cho, D.-U. Kim, and J. H. Kehrl RGS14 Is a Centrosomal and Nuclear Cytoplasmic Shuttling Protein That Traffics to Promyelocytic Leukemia Nuclear Bodies Following Heat Shock J. Biol. Chem., January 7, 2005; 280(1): 805 - 814. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
V. Mittal and M. E. Linder The RGS14 GoLoco Domain Discriminates among G{alpha}i Isoforms J. Biol. Chem., November 5, 2004; 279(45): 46772 - 46778. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 G.-X. Shi, K. Harrison, S.-B. Han, C. Moratz, and J. H. Kehrl Toll-Like Receptor Signaling Alters the Expression of Regulator of G Protein Signaling Proteins in Dendritic Cells: Implications for G Protein-Coupled Receptor Signaling J. Immunol., May 1, 2004; 172(9): 5175 - 5184. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
E. Lippert, D. L. Yowe, J.-A. Gonzalo, J. P. Justice, J. M. Webster, E. R. Fedyk, M. Hodge, C. Miller, J.-C. Gutierrez-Ramos, F. Borrego, et al. Role of Regulator of G Protein Signaling 16 in Inflammation- Induced T Lymphocyte Migration and Activation J. Immunol., August 1, 2003; 171(3): 1542 - 1555. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 S. Hollinger and J. R. Hepler Cellular Regulation of RGS Proteins: Modulators and Integrators of G Protein Signaling Pharmacol. Rev., September 1, 2002; 54(3): 527 - 559. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
F. Liao, A.-K. Shirakawa, J. F. Foley, R. L. Rabin, and J. M. Farber Human B Cells Become Highly Responsive to Macrophage-Inflammatory Protein-3{alpha}/CC Chemokine Ligand-20 After Cellular Activation Without Changes in CCR6 Expression or Ligand Binding J. Immunol., May 15, 2002; 168(10): 4871 - 4880. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
S. Evellin, J. Nolte, K. Tysack, F. vom Dorp, M. Thiel, P. A. O. Weernink, K. H. Jakobs, E. J. Webb, J. W. Lomasney, and M. Schmidt Stimulation of Phospholipase C-epsilon by the M3 Muscarinic Acetylcholine Receptor Mediated by Cyclic AMP and the GTPase Rap2B J. Biol. Chem., May 3, 2002; 277(19): 16805 - 16813. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 H. Zhong and R. R. Neubig Regulator of G Protein Signaling Proteins: Novel Multifunctional Drug Targets J. Pharmacol. Exp. Ther., June 1, 2001; 297(3): 837 - 845. [Abstract] [Full Text]
|
|
|
|
|
|
R. J. Kimple, L. De Vries, H. Tronchere, C. I. Behe, R. A. Morris, M. G. Farquhar, and D. P. Siderovski RGS12 and RGS14 GoLoco Motifs Are Galpha i Interaction Sites with Guanine Nucleotide Dissociation Inhibitor Activity J. Biol. Chem., July 27, 2001; 276(31): 29275 - 29281. [Abstract] [Full Text] [PDF]
|
|
 |
 |
 |
|
 |
 |
 |
