TY - JOUR
T1 - Flexible functional interactions between G-protein subunits contribute to the specificity of plant responses
AU - Roy Choudhury, Swarup
AU - Li, Mao
AU - Lee, Veronica
AU - Nandety, Raja Sekhar
AU - Mysore, Kirankumar S.
AU - Pandey, Sona
N1 - Funding Information:
The authors sincerely thank Elizabeth (Toby) Kellogg (DDPSC) for helpful discussion and critical comments on the manuscript and Blake Meyers (DDPSC) and Elizabeth Haswell (Washington University, St. Louis, USA) for the help with generation of CRISPR‐Cas9 mutant lines. Research in the author’s laboratory is supported by NIFA/AFRI (2015‐67013‐22964) and NSF (IOS‐1557942 and MCB‐1714693) grants. KSM acknowledges funding from Noble Research Institute.
Publisher Copyright:
© 2020 Society for Experimental Biology and John Wiley & Sons Ltd
PY - 2020/4/1
Y1 - 2020/4/1
N2 - Plants being sessile integrate information from a variety of endogenous and external cues simultaneously to optimize growth and development. This necessitates the signaling networks in plants to be highly dynamic and flexible. One such network involves heterotrimeric G-proteins comprised of Gα, Gβ, and Gγ subunits, which influence many aspects of growth, development, and stress response pathways. In plants such as Arabidopsis, a relatively simple repertoire of G-proteins comprised of one canonical and three extra-large Gα, one Gβ and three Gγ subunits exists. Because the Gβ and Gγ proteins form obligate dimers, the phenotypes of plants lacking the sole Gβ or all Gγ genes are similar, as expected. However, Gα proteins can exist either as monomers or in a complex with Gβγ, and the details of combinatorial genetic and physiological interactions of different Gα proteins with the sole Gβ remain unexplored. To evaluate such flexible, signal-dependent interactions and their contribution toward eliciting a specific response, we have generated Arabidopsis mutants lacking specific combinations of Gα and Gβ genes, performed extensive phenotypic analysis, and evaluated the results in the context of subunit usage and interaction specificity. Our data show that multiple mechanistic modes, and in some cases complex epistatic relationships, exist depending on the signal-dependent interactions between the Gα and Gβ proteins. This suggests that, despite their limited numbers, the inherent flexibility of plant G-protein networks provides for the adaptability needed to survive under continuously changing environments.
AB - Plants being sessile integrate information from a variety of endogenous and external cues simultaneously to optimize growth and development. This necessitates the signaling networks in plants to be highly dynamic and flexible. One such network involves heterotrimeric G-proteins comprised of Gα, Gβ, and Gγ subunits, which influence many aspects of growth, development, and stress response pathways. In plants such as Arabidopsis, a relatively simple repertoire of G-proteins comprised of one canonical and three extra-large Gα, one Gβ and three Gγ subunits exists. Because the Gβ and Gγ proteins form obligate dimers, the phenotypes of plants lacking the sole Gβ or all Gγ genes are similar, as expected. However, Gα proteins can exist either as monomers or in a complex with Gβγ, and the details of combinatorial genetic and physiological interactions of different Gα proteins with the sole Gβ remain unexplored. To evaluate such flexible, signal-dependent interactions and their contribution toward eliciting a specific response, we have generated Arabidopsis mutants lacking specific combinations of Gα and Gβ genes, performed extensive phenotypic analysis, and evaluated the results in the context of subunit usage and interaction specificity. Our data show that multiple mechanistic modes, and in some cases complex epistatic relationships, exist depending on the signal-dependent interactions between the Gα and Gβ proteins. This suggests that, despite their limited numbers, the inherent flexibility of plant G-protein networks provides for the adaptability needed to survive under continuously changing environments.
KW - Arabidopsis thaliana
KW - extra-large G-proteins
KW - G-protein β-subunit
KW - heterotrimeric G-proteins
UR - http://www.scopus.com/inward/record.url?scp=85081751965&partnerID=8YFLogxK
U2 - 10.1111/tpj.14714
DO - 10.1111/tpj.14714
M3 - Article
C2 - 32034949
AN - SCOPUS:85081751965
SN - 0960-7412
VL - 102
SP - 207
EP - 221
JO - Plant Journal
JF - Plant Journal
IS - 2
ER -