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Title: Extra Large G-Protein Interactome Reveals Multiple Stress Response Function and Partner-Dependent XLG Subcellular Localization

Journal Article · · Frontiers in Plant Science
 [1];  [2];  [3]
  1. Northwest A&F Univ., Xianyang (China). College of Natural Resources and Environment; Univ. of North Carolina, Chapel Hill, NC (United States). Dept. of Biology
  2. Northwest A&F Univ., Xianyang (China). College of Natural Resources and Environment
  3. Univ. of North Carolina, Chapel Hill, NC (United States). Dept. of Biology and Dept. of Pharmacology

The three-member family of Arabidopsis extra-large G proteins (XLG1-3) defines the prototype of an atypical Ga subunit in the heterotrimeric G protein complex. Some recent evidence indicate that XLG subunits operate along with its Gbg dimer in root morphology, stress responsiveness, and cytokinin induced development, however downstream targets of activated XLG proteins in the stress pathways are rarely known. In order to assemble a set of candidate XLG-targeted proteins, a yeast two-hybrid complementation-based screen was performed using XLG protein baits to query interactions between XLG and partner protein found in glucose-treated seedlings, roots, and Arabidopsis cells in culture. Seventy two interactors were identified and >60% of a test set displayed in vivo interaction with XLG proteins. Gene co-expression analysis shows that >70% of the interactors are positively correlated with the corresponding XLG partners. Gene Ontology enrichment for all the candidates indicates stress responses and posits a molecular mechanism involving a specific set of transcription factor partners to XLG. Genes encoding two of these transcription factors, SZF1 and 2, require XLG proteins for full NaCl-induced expression. Furthermore, the subcellular localization of the XLG proteins in the nucleus, endosome, and plasma membrane is dependent on the specific interacting partner.

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; R01GM065989; MCB-0718202
OSTI ID:
1374569
Journal Information:
Frontiers in Plant Science, Vol. 8; ISSN 1664-462X
Publisher:
Frontiers Research FoundationCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 24 works
Citation information provided by
Web of Science

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Cited By (4)

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Development and cell death domain-containing asparagine-rich protein (DCD/NRP): an essential protein in plant development and stress responses journal December 2018
GCR1 and GPA1 coupling regulates nitrate, cell wall, immunity and light responses in Arabidopsis journal April 2019
Genetic and Systematic Approaches Toward G Protein-Coupled Abiotic Stress Signaling in Plants journal September 2018