FEBS Letters
Volume 582, Issue 25 , Pages 3577-3584, 29 October 2008

d-Glucose sensing by a plasma membrane regulator of G signaling protein, AtRGS1

Edited by Micheal R. Sussman

  • Jeffrey C. Grigston

      Affiliations

    • Department of Biology, CB#3280, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280, USA
  • ,
  • Daniel Osuna

      Affiliations

    • Max Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany
  • ,
  • Wolf-Rüdiger Scheible

      Affiliations

    • Max Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany
  • ,
  • Chenggang Liu

      Affiliations

    • Department of Biology, CB#3280, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280, USA
  • ,
  • Mark Stitt

      Affiliations

    • Max Planck Institute of Molecular Plant Physiology, 14476 Potsdam-Golm, Germany
  • ,
  • Alan M. Jones

      Affiliations

    • Department of Biology, CB#3280, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280, USA
    • Department of Pharmacology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA
    • Corresponding Author InformationCorresponding author. Address: Department of Biology, CB#3280, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599-3280, USA. Fax: +1 919 962 1625.

Received 11 July 2008; received in revised form 22 August 2008; accepted 25 August 2008. published online 23 September 2008.

Abstract 

Plants use sugars as signaling molecules and possess mechanisms to detect and respond to changes in sugar availability, ranging from the level of secondary signaling molecules to altered gene transcription. G-protein-coupled pathways are involved in sugar signaling in plants. The Arabidopsis thaliana regulator of G-protein signaling protein 1 (AtRGS1) combines a receptor-like seven transmembrane domain with an RGS domain, interacts with the Arabidopsis Gα subunit (AtGPA1) in a d-glucose-regulated manner, and stimulates AtGPA1 GTPase activity. We determined that AtRGS1 interacts with additional components, genetically defined here, to serve as a plasma membrane sensor for d-glucose. This interaction between AtRGS1 and AtGPA1 involves, in part, the seven-transmembrane domain of AtRGS1.

Structured summary


MINT-6743118:

RGS1 (uniprotkb:Q8H1F2) and

GPA1 (uniprotkb:P18064) physically interact (MI:0218) by bimolecular fluorescence complementation (MI:0809)

Keywords: Arabidopsis thaliana regulator of G-protein signaling protein 1, Glucose sensing, Heterotrimeric G protein complex, Regulator of G signaling protein 1, Arabidopsis

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PII: S0014-5793(08)00755-2

doi:10.1016/j.febslet.2008.08.038

FEBS Letters
Volume 582, Issue 25 , Pages 3577-3584, 29 October 2008