scholarly journals Gα13 Mediates a Signal That Is Essential for Proliferation and Survival of Thymocyte Progenitors

2004 ◽  
Vol 200 (10) ◽  
pp. 1315-1324 ◽  
Author(s):  
V. McNeil Coffield ◽  
Whitney S. Helms ◽  
Qi Jiang ◽  
Lishan Su
Keyword(s):  
T Cell ◽  
Progenitor Cells ◽  
G Protein ◽  
Cell Receptor ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Organ Cultures ◽  
Fetal Thymus ◽  
Thymocyte Proliferation ◽  
Signaling Domain

G protein signaling via the Gα12 family (Gα12 and Gα13) has not been well studied in T cells. To investigate whether Gα12 and Gα13 are involved in thymopoiesis, we expressed the regulator of G protein signaling domain of p115RhoGEF to inhibit Gα12 and Gα13 during thymopoiesis. Fetal thymus organ cultures seeded with p115ΔDH-expressing progenitor cells showed impaired thymopoiesis with a block at the CD4−CD8−CD44−CD25+ (DN3) stage. Using Gα13 or Gα12 minigenes, we demonstrated that Gα13, but not Gα12, is required for thymopoiesis. T progenitor cells expressing p115ΔDH showed reduced proliferation and increased cell death. T cell receptor stimulation of the fetal thymus organ cultures did not rescue the block. Overexpression of the antiapoptotic gene Bcl2 rescued the defect in DN3 cells and partially rescued T cell development. Therefore, Gα13-mediated signaling is necessary in early thymocyte proliferation and survival.

scholarly journals Cutting Edge: Regulator of G Protein Signaling-1 Selectively Regulates Gut T Cell Trafficking and Colitic Potential

2011 ◽  
Vol 187 (5) ◽  
pp. 2067-2071 ◽  
Author(s):  
Deena L. Gibbons ◽  
Lucie Abeler-Dörner ◽  
Tim Raine ◽  
Il-Young Hwang ◽  
Anett Jandke ◽  
...  
Keyword(s):  
T Cell ◽  
G Protein ◽  
Cutting Edge ◽  
G Protein Signaling ◽  
Cell Trafficking ◽  
Protein Signaling ◽  
T Cell Trafficking

The Regulator of G Protein Signaling Domain of Axin Selectively Interacts with Gα12 but Not Gα13

2006 ◽  
Vol 70 (4) ◽  
pp. 1461-1468 ◽  
Author(s):  
Laura N. Stemmle ◽  
Timothy A. Fields ◽  
Patrick J. Casey
Keyword(s):  
G Protein ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Signaling Domain

scholarly journals Role of the RGS (regulator of G-protein signaling) domain of axin in vertebrate axis formation

2006 ◽  
Vol 295 (1) ◽  
pp. 435
Author(s):  
Patricia N. Schneider ◽  
Diane C. Slusarski ◽  
Douglas W. Houston
Keyword(s):  
G Protein ◽  
Axis Formation ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Signaling Domain

scholarly journals Extragenic Suppressors of Loss-of-Function Mutations in the Aspergillus FlbA Regulator of G-Protein Signaling Domain Protein

Genetics ◽  
1999 ◽  
Vol 151 (1) ◽  
pp. 97-105 ◽  
Author(s):  
Jae-Hyuk Yu ◽  
Stefan Rosén ◽  
Thomas H Adams
Keyword(s):  
G Protein ◽  
Growth Control ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Loss Of Function ◽  
Α Subunit ◽  
Suppressor Mutations ◽  
Rgs Domain ◽  
Signaling Domain ◽  
Domain Protein

Abstract We showed previously that two genes, flbA and fadA, have a major role in determining the balance between growth, sporulation, and mycotoxin (sterigmatocystin; ST) production by the filamentous fungus Aspergillus nidulans. fadA encodes the α subunit for a heterotrimeric G-protein, and continuous activation of FadA blocks sporulation and ST production while stimulating growth. flbA encodes an A. nidulans regulator of G-protein signaling (RGS) domain protein that antagonizes FadA-mediated signaling to allow development. To better understand FlbA function and other aspects of FadA-mediated growth control, we have isolated and characterized mutations in four previously undefined genes designated as sfaA, sfaC, sfaD, and sfaE (suppressors of flbA), and a new allele of fadA (fadAR205H), all of which suppress a flbA loss-of-function mutation (flbA98). These suppressors overcome flbA losses of function in both sporulation and ST biosynthesis. fadAR205H, sfaC67, sfaD82, and sfaE83 mutations are dominant to wild type whereas sfaA1 is semidominant. sfaA1 also differs from other suppressor mutations in that it cannot suppress a flbA deletion mutation (and is therefore allele specific) whereas all the dominant suppressors can bypass complete loss of flbA. Only sfaE83 suppressed dominant activating mutations in fadA, indicating that sfaE may have a unique role in fadA-flbA interactions. Finally, none of these suppressor mutations bypassed fluG loss-of-function mutations in development-specific activation.

scholarly journals RGS3 controls T lymphocyte migration in a model of Th2-mediated airway inflammation

2013 ◽  
Vol 305 (10) ◽  
pp. L693-L701 ◽  
Author(s):  
Jesse W. Williams ◽  
Douglas Yau ◽  
Nan Sethakorn ◽  
Jacob Kach ◽  
Eleanor B. Reed ◽  
...  
Keyword(s):  
T Cells ◽  
Cell Migration ◽  
T Cell ◽  
Immune Responses ◽  
G Protein ◽  
G Protein Signaling ◽  
Protein Signaling ◽  
Cell Numbers ◽  
T Cell Migration

T cell migration toward sites of antigen exposure is mediated by G protein signaling and is a key function in the development of immune responses. Regulators of G protein signaling (RGS) proteins modulate G protein signaling; however, their role in the regulation of adaptive immune responses has not been thoroughly explored. Herein we demonstrated abundant expression of the Gi/Gq-specific RGS3 in activated T cells, and that diminished RGS3 expression in a T cell thymoma increased cytokine-induced migration. To examine the role of endogenous RGS3 in vivo, mice deficient in the RGS domain (RGS3ΔRGS) were generated and tested in an experimental model of asthma. Compared with littermate controls, the inflammation in the RGS3ΔRGS mice was characterized by increased T cell numbers and the striking development of perivascular lymphoid structures. Surprisingly, while innate inflammatory cells were also increased in the lungs of RGS3ΔRGS mice, eosinophil numbers and Th2 cytokine production were equivalent to control mice. In contrast, T cell numbers in the draining lymph nodes (dLN) were reduced in the RGS3ΔRGS, demonstrating a redistribution of T cells from the dLN to the lungs via increased RGS3ΔRGS T cell migration. Together these novel findings show a nonredundant role for endogenous RGS3 in controlling T cell migration in vitro and in an in vivo model of inflammation.

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