Glutathione upregulates cAMP signalling via G protein alpha 2 during the development of Dictyostelium discoideum

Despite the importance of glutathione in Dictyostelium, the role of glutathione synthetase (gshB/GSS) has not been clearly investigated. In this study, we observed that increasing glutathione content by constitutive expression of gshB leads to mound‐arrest and defects in 3′,5′‐cyclic adenosine monop...

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Bibliographic Details
Published in:FEBS letters 2016-12, Vol.590 (23), p.4361-4371
Main Authors: Lee, Hyang‐Mi, Kim, Ji‐Sun, Kang, Sa‐Ouk
Format: Article
Language:English
Subjects:
cAMP signalling
Cell Membrane - metabolism
Cyclic AMP - metabolism
Dictyostelium - cytology
Dictyostelium - genetics
Dictyostelium - growth & development
Dictyostelium - metabolism
G protein alpha 2
Gene Knockdown Techniques
glutathione
Glutathione - metabolism
Glutathione Synthase - genetics
GTP-Binding Protein alpha Subunit, Gi2 - deficiency
GTP-Binding Protein alpha Subunit, Gi2 - genetics
GTP-Binding Protein alpha Subunit, Gi2 - metabolism
Intracellular Space - metabolism
Signal Transduction
Up-Regulation
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Summary:Despite the importance of glutathione in Dictyostelium, the role of glutathione synthetase (gshB/GSS) has not been clearly investigated. In this study, we observed that increasing glutathione content by constitutive expression of gshB leads to mound‐arrest and defects in 3′,5′‐cyclic adenosine monophosphate (cAMP)‐mediated aggregation and developmental gene expression. The overexpression of gpaB encoding G protein alpha 2 (Gα2), an essential component of the cAMP signalling pathway, results in a phenotype similar to that caused by gshB overexpression, whereas gpaB knockdown in gshB‐overexpressing cells partially rescues the above‐mentioned phenotypic defects. Furthermore, Gα2 is highly enriched at the plasma membrane of gshB‐overexpressing cells compared to wild‐type cells. Therefore, our findings suggest that glutathione upregulates cAMP signalling via Gα2 modulation during Dictyostelium development.
ISSN:0014-5793
1873-3468
DOI:10.1002/1873-3468.12453