Cargando…
Phosphorylation of RGS regulates MAP kinase localization and promotes completion of cytokinesis
Yeast use the G-protein–coupled receptor signaling pathway to detect and track the mating pheromone. The G-protein–coupled receptor pathway is inhibited by the regulator of G-protein signaling (RGS) Sst2 which induces Gα GTPase activity and inactivation of downstream signaling. G-protein signaling a...
Autores principales: | , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Life Science Alliance LLC
2022
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9394524/ https://www.ncbi.nlm.nih.gov/pubmed/35985794 http://dx.doi.org/10.26508/lsa.202101245 |
_version_ | 1784771508699136000 |
---|---|
author | Simke, William C Johnson, Cory P Hart, Andrew J Mayhue, Sari Craig, P Lucas Sojka, Savannah Kelley, Joshua B |
author_facet | Simke, William C Johnson, Cory P Hart, Andrew J Mayhue, Sari Craig, P Lucas Sojka, Savannah Kelley, Joshua B |
author_sort | Simke, William C |
collection | PubMed |
description | Yeast use the G-protein–coupled receptor signaling pathway to detect and track the mating pheromone. The G-protein–coupled receptor pathway is inhibited by the regulator of G-protein signaling (RGS) Sst2 which induces Gα GTPase activity and inactivation of downstream signaling. G-protein signaling activates the MAPK Fus3, which phosphorylates the RGS; however, the role of this modification is unknown. We found that pheromone-induced RGS phosphorylation peaks early; the phospho-state of RGS controls its localization and influences MAPK spatial distribution. Surprisingly, phosphorylation of the RGS promotes completion of cytokinesis before pheromone-induced growth. Completion of cytokinesis in the presence of pheromone is promoted by the kelch-repeat protein, Kel1 and antagonized by the formin Bni1. We found that RGS complexes with Kel1 and prefers the unphosphorylatable RGS mutant. We also found overexpression of unphosphorylatable RGS exacerbates cytokinetic defects, whereas they are rescued by overexpression of Kel1. These data lead us to a model where Kel1 promotes completion of cytokinesis before pheromone-induced polarity but is inhibited by unphosphorylated RGS binding. |
format | Online Article Text |
id | pubmed-9394524 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | Life Science Alliance LLC |
record_format | MEDLINE/PubMed |
spelling | pubmed-93945242022-09-02 Phosphorylation of RGS regulates MAP kinase localization and promotes completion of cytokinesis Simke, William C Johnson, Cory P Hart, Andrew J Mayhue, Sari Craig, P Lucas Sojka, Savannah Kelley, Joshua B Life Sci Alliance Research Articles Yeast use the G-protein–coupled receptor signaling pathway to detect and track the mating pheromone. The G-protein–coupled receptor pathway is inhibited by the regulator of G-protein signaling (RGS) Sst2 which induces Gα GTPase activity and inactivation of downstream signaling. G-protein signaling activates the MAPK Fus3, which phosphorylates the RGS; however, the role of this modification is unknown. We found that pheromone-induced RGS phosphorylation peaks early; the phospho-state of RGS controls its localization and influences MAPK spatial distribution. Surprisingly, phosphorylation of the RGS promotes completion of cytokinesis before pheromone-induced growth. Completion of cytokinesis in the presence of pheromone is promoted by the kelch-repeat protein, Kel1 and antagonized by the formin Bni1. We found that RGS complexes with Kel1 and prefers the unphosphorylatable RGS mutant. We also found overexpression of unphosphorylatable RGS exacerbates cytokinetic defects, whereas they are rescued by overexpression of Kel1. These data lead us to a model where Kel1 promotes completion of cytokinesis before pheromone-induced polarity but is inhibited by unphosphorylated RGS binding. Life Science Alliance LLC 2022-08-19 /pmc/articles/PMC9394524/ /pubmed/35985794 http://dx.doi.org/10.26508/lsa.202101245 Text en © 2022 Simke et al. https://creativecommons.org/licenses/by/4.0/This article is available under a Creative Commons License (Attribution 4.0 International, as described at https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Research Articles Simke, William C Johnson, Cory P Hart, Andrew J Mayhue, Sari Craig, P Lucas Sojka, Savannah Kelley, Joshua B Phosphorylation of RGS regulates MAP kinase localization and promotes completion of cytokinesis |
title | Phosphorylation of RGS regulates MAP kinase localization and promotes completion of cytokinesis |
title_full | Phosphorylation of RGS regulates MAP kinase localization and promotes completion of cytokinesis |
title_fullStr | Phosphorylation of RGS regulates MAP kinase localization and promotes completion of cytokinesis |
title_full_unstemmed | Phosphorylation of RGS regulates MAP kinase localization and promotes completion of cytokinesis |
title_short | Phosphorylation of RGS regulates MAP kinase localization and promotes completion of cytokinesis |
title_sort | phosphorylation of rgs regulates map kinase localization and promotes completion of cytokinesis |
topic | Research Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9394524/ https://www.ncbi.nlm.nih.gov/pubmed/35985794 http://dx.doi.org/10.26508/lsa.202101245 |
work_keys_str_mv | AT simkewilliamc phosphorylationofrgsregulatesmapkinaselocalizationandpromotescompletionofcytokinesis AT johnsoncoryp phosphorylationofrgsregulatesmapkinaselocalizationandpromotescompletionofcytokinesis AT hartandrewj phosphorylationofrgsregulatesmapkinaselocalizationandpromotescompletionofcytokinesis AT mayhuesari phosphorylationofrgsregulatesmapkinaselocalizationandpromotescompletionofcytokinesis AT craigplucas phosphorylationofrgsregulatesmapkinaselocalizationandpromotescompletionofcytokinesis AT sojkasavannah phosphorylationofrgsregulatesmapkinaselocalizationandpromotescompletionofcytokinesis AT kelleyjoshuab phosphorylationofrgsregulatesmapkinaselocalizationandpromotescompletionofcytokinesis |