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Title: Evidence for an unusual transmembrane configuration of AGG3, a class C Gγ subunit of Arabidopsis

Journal Article · · The Plant Journal
DOI:https://doi.org/10.1111/tpj.12732· OSTI ID:1344923
 [1];  [2];  [1];  [1];  [3];  [4];  [4];  [5];  [1];  [3]
  1. Univ. of North Carolina, Chapel Hill, NC (United States)
  2. Univ. of Queensland, Brisbane (Australia); Pennsylvania State Univ., University Park, PA (United States)
  3. Univ. of Queensland, Brisbane (Australia)
  4. Univ. of Newcastle, Callaghan, NSW (Australia)
  5. Pennsylvania State Univ., University Park, PA (United States)
+ Show Author Affiliations

Summary Heterotrimeric G  proteins are crucial for the perception of external signals and subsequent signal transduction in animal and plant cells. In both model systems, the complex comprises one G α, one G β, and one G γ subunit. However, in addition to the canonical G γ subunits (class  A ), plants also possess two unusual, plant‐specific classes of G γ subunits (classes B and C ) that have not yet been found in animals. These include G γ subunits lacking the C –terminal C aa X motif (class  B ), which is important for membrane anchoring of the protein; the presence of such subunits gives rise to a flexible sub‐population of G β/γ heterodimers that are not necessarily restricted to the plasma membrane. Plants also contain class  C G γ subunits, which are twice the size of canonical G γ subunits, with a predicted transmembrane domain and a large cysteine‐rich extracellular C –terminus. However, neither the presence of the transmembrane domain nor the membrane topology have been unequivocally demonstrated. Here, we provide compelling evidence that AGG 3, a class  C G γ subunit of A rabidopsis, contains a functional transmembrane domain, which is sufficient but not essential for plasma membrane localization, and that the cysteine‐rich C –terminus is extracellular.

Research Organization:
University of North Carolina, Chapel Hill, NC (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Basic Energy Sciences (BES)
Grant/Contract Number:
FG02-05er15671
OSTI ID:
1344923
Alternate ID(s):
OSTI ID: 1400679
Journal Information:
The Plant Journal, Vol. 81, Issue 3; ISSN 0960-7412
Publisher:
Society for Experimental BiologyCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 23 works
Citation information provided by
Web of Science

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GTPase acceleration as the rate-limiting step in Arabidopsis G protein-coupled sugar signaling text January 2007

Cited By (8)

Mutation of RGG 2 , which encodes a type B heterotrimeric G protein γ subunit, increases grain size and yield production in rice journal December 2018
Multi-functionality of proteins involved in GPCR and G protein signaling: making sense of structure–function continuum with intrinsic disorder-based proteoforms journal August 2019
Nucleotide exchange–dependent and nucleotide exchange–independent functions of plant heterotrimeric GTP-binding proteins journal November 2019
Heterotrimeric G-Protein-Dependent Proteome and Phosphoproteome in Unstimulated Arabidopsis Roots journal December 2018
Heterotrimeric G protein are involved in the regulation of multiple agronomic traits and stress tolerance in rice journal February 2020
Plant Morphology of Heterotrimeric G Protein Mutants journal January 2016
Plant Morphology of Heterotrimeric G Protein Mutants text January 2016
Plant G-Proteins Come of Age: Breaking the Bond with Animal Models journal May 2016

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Related Subjects

59 BASIC BIOLOGICAL SCIENCES
Arabidopsis Gγ subunit 3
AGG3
membrane topology
Heterotrimeric G protein
Arabidopsis thaliana