MAPK docking motif in the Dictyostelium Gα2 subunit is required for aggregation and transcription factor translocation.
MAPK docking motif in the Dictyostelium Gα2 subunit is required for aggregation and transcription factor translocation.
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DOI:
10.1016/j.cellsig.2021.110117
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发表时间:
2021-11
影响因子:
4.8
通讯作者:
Hadwiger JA
中科院分区:
文献类型:
--
作者:
Adhikari N;McGill IN;Hadwiger JA
Some G protein alpha subunits contain a mitogen-activated protein kinase (MAPK) docking motif (D-motif) near the amino terminus that can impact cellular responses to external signals. The Dictyostelium Gα2 G protein subunit is required for chemotaxis to cAMP during the onset of multicellular development and this subunit contains a putative D-motif near the amino terminus. The Gα2 subunit D-motif was altered to examine its potential role in chemotaxis and multicellular development. In gα2− cells the expression of the D-motif mutant (Gα2D−) or wild-type subunit from high copy number vectors rescued cell aggregation but blocked the transition of mounds into slugs. This phenotype was also observed in parental strains with a wild-type gα2 locus indicating that the heterologous Gα2 subunit expression interferes with multicellular morphogenesis. Expression of the Gα2D− subunit from a low copy number vectors in gα2− cells did not rescue aggregation whereas the wild-type Gα2 subunit rescued aggregation efficiently and allowed wild-type morphological development. The Gα2D− and Gα2 subunit were both capable of restoring comparable levels of cAMP stimulated motility and the ability to co-aggregate with wild-type cells implying that the aggregation defect of Gα2D− expressing cells is due to insufficient intercellular signaling. Expression of the Gα2 subunit but not the Gα2D− subunit fully restored the ability of cAMP to stimulate the translocation of the GtaC transcription factor suggesting the D-motif is important for transcription factor regulation. These results suggest that the D-motif of Gα2 plays a role in aggregation and other developmental responses involved with cAMP signaling.
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