Dose-Duration Reciprocity for G protein activation: Modulation of kinase to substrate ratio alters cell signaling.
In animal cells, activation of heterotrimeric G protein signaling generally occurs when the system's cognate signal exceeds a threshold, whereas in plant cells, both the amount and the exposure time of at least one signal, D-glucose, are used toward activation. This unusual signaling property c...
| Main Authors: | , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2017-01-01
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| Series: | PLoS ONE |
| Online Access: | https://doi.org/10.1371/journal.pone.0190000 |
| _version_ | 1818405134401536000 |
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| author | Kang-Ling Liao Charles E Melvin Rosangela Sozzani Roger D Jones Timothy C Elston Alan M Jones |
| author_facet | Kang-Ling Liao Charles E Melvin Rosangela Sozzani Roger D Jones Timothy C Elston Alan M Jones |
| author_sort | Kang-Ling Liao |
| collection | DOAJ |
| description | In animal cells, activation of heterotrimeric G protein signaling generally occurs when the system's cognate signal exceeds a threshold, whereas in plant cells, both the amount and the exposure time of at least one signal, D-glucose, are used toward activation. This unusual signaling property called Dose-Duration Reciprocity, first elucidated in the genetic model Arabidopsis thaliana, is achieved by a complex that is comprised of a 7-transmembrane REGULATOR OF G SIGNALING (RGS) protein (AtRGS1), a Gα subunit that binds and hydrolyzes nucleotide, a Gβγ dimer, and three WITH NO LYSINE (WNK) kinases. D-glucose is one of several signals such as salt and pathogen-derived molecular patterns that operates through this protein complex to activate G protein signaling by WNK kinase transphosphorylation of AtRGS1. Because WNK kinases compete for the same substrate, AtRGS1, we hypothesize that activation is sensitive to the AtRGS1 amount and that modulation of the AtRGS1 pool affects the response to the stimulant. Mathematical simulation revealed that the ratio of AtRGS1 to the kinase affects system sensitivity to D-glucose, and therefore illustrates how modulation of the cellular AtRGS1 level is a means to change signal-induced activation. AtRGS1 levels change under tested conditions that mimic physiological conditions therefore, we propose a previously-unknown mechanism by which plants react to changes in their environment. |
| first_indexed | 2024-12-14T08:51:13Z |
| format | Article |
| id | doaj.art-7ba5cb5121ce4f2ea8bb2ec5716aeabb |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-14T08:51:13Z |
| publishDate | 2017-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-7ba5cb5121ce4f2ea8bb2ec5716aeabb2022-12-21T23:09:03ZengPublic Library of Science (PLoS)PLoS ONE1932-62032017-01-011212e019000010.1371/journal.pone.0190000Dose-Duration Reciprocity for G protein activation: Modulation of kinase to substrate ratio alters cell signaling.Kang-Ling LiaoCharles E MelvinRosangela SozzaniRoger D JonesTimothy C ElstonAlan M JonesIn animal cells, activation of heterotrimeric G protein signaling generally occurs when the system's cognate signal exceeds a threshold, whereas in plant cells, both the amount and the exposure time of at least one signal, D-glucose, are used toward activation. This unusual signaling property called Dose-Duration Reciprocity, first elucidated in the genetic model Arabidopsis thaliana, is achieved by a complex that is comprised of a 7-transmembrane REGULATOR OF G SIGNALING (RGS) protein (AtRGS1), a Gα subunit that binds and hydrolyzes nucleotide, a Gβγ dimer, and three WITH NO LYSINE (WNK) kinases. D-glucose is one of several signals such as salt and pathogen-derived molecular patterns that operates through this protein complex to activate G protein signaling by WNK kinase transphosphorylation of AtRGS1. Because WNK kinases compete for the same substrate, AtRGS1, we hypothesize that activation is sensitive to the AtRGS1 amount and that modulation of the AtRGS1 pool affects the response to the stimulant. Mathematical simulation revealed that the ratio of AtRGS1 to the kinase affects system sensitivity to D-glucose, and therefore illustrates how modulation of the cellular AtRGS1 level is a means to change signal-induced activation. AtRGS1 levels change under tested conditions that mimic physiological conditions therefore, we propose a previously-unknown mechanism by which plants react to changes in their environment.https://doi.org/10.1371/journal.pone.0190000 |
| spellingShingle | Kang-Ling Liao Charles E Melvin Rosangela Sozzani Roger D Jones Timothy C Elston Alan M Jones Dose-Duration Reciprocity for G protein activation: Modulation of kinase to substrate ratio alters cell signaling. PLoS ONE |
| title | Dose-Duration Reciprocity for G protein activation: Modulation of kinase to substrate ratio alters cell signaling. |
| title_full | Dose-Duration Reciprocity for G protein activation: Modulation of kinase to substrate ratio alters cell signaling. |
| title_fullStr | Dose-Duration Reciprocity for G protein activation: Modulation of kinase to substrate ratio alters cell signaling. |
| title_full_unstemmed | Dose-Duration Reciprocity for G protein activation: Modulation of kinase to substrate ratio alters cell signaling. |
| title_short | Dose-Duration Reciprocity for G protein activation: Modulation of kinase to substrate ratio alters cell signaling. |
| title_sort | dose duration reciprocity for g protein activation modulation of kinase to substrate ratio alters cell signaling |
| url | https://doi.org/10.1371/journal.pone.0190000 |
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