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Dose-Duration Reciprocity for G protein activation: Modulation of kinase to substrate ratio alters cell signaling

Journal Article · · PLoS ONE
 [1];  [2];  [2];  [3];  [4];  [5]
  1. Univ. of North Carolina, Chapel Hill, NC (United States). Dept. of Biology; OSTI
  2. Univ. of North Carolina, Chapel Hill, NC (United States). Dept. of Plant and Microbial Biology
  3. Stevens Inst. of Technology, Hoboken, NJ (United States)
  4. Univ. of North Carolina, Chapel Hill, NC (United States). Dept. of Pharmacology
  5. Univ. of North Carolina, Chapel Hill, NC (United States). Dept. of Biology, and Dept. of Pharmacology
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.
Research Organization:
Univ. of North Carolina, Chapel Hill, NC (United States)
Sponsoring Organization:
USDOE
Grant/Contract Number:
FG02-05ER15671
OSTI ID:
1499880
Journal Information:
PLoS ONE, Journal Name: PLoS ONE Journal Issue: 12 Vol. 12; ISSN 1932-6203
Publisher:
Public Library of ScienceCopyright Statement
Country of Publication:
United States
Language:
English

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Long-distance communication in Arabidopsis involving a self-activating G protein journal February 2018

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