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The Signalling Function of Plant GTP-Binding Proteins
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The Signalling Function of Plant GTP-Binding Proteins

A special issue of Plants (ISSN 2223-7747). This special issue belongs to the section "Plant Physiology and Metabolism".

Deadline for manuscript submissions: closed (28 February 2022) | Viewed by 10644

Special Issue Editor

Prof. Dr. Attila Fehér

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Guest Editor
1. Department of Plant Biology, Faculty of Science and Informatics, University of Szeged, 52. Közép fasor, H-6726 Szeged, Hungary
2. Institute of Plant Biology, Biological Research Center, 62. Temesvári krt., H-6726 Szeged, Hungary
Interests: plant molecular biology; plant cell biology; plant developmental biology; plant genetic engineering; plant biotechnology; kinase signaling; small GTPase signaling; plant embryogenesis; in vitro plant regeneration; plant cell division; plant cell differentiation; Arabidopsis thaliana
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Special Issue Information

Dear Colleagues, 

GTP-binding proteins are central in various processes determining plant shape and function, including environmental adaptation. These versatile signalling molecules can interact with the plethora of upstream regulators and downstream effectors. In this way, they are capable of integrating various hormonal, developmental and abiotic/biotic stress signalling pathways. At the cellular level, they control the size, shape and polarity of cells organising primarily the cytoskeleton, vesicular transport, and gene expression. Despite the accumulating experimental data signifying the role of GTPases and their interacting proteins in plant development and adaptation, our knowledge about the associated signalling pathways is still scarce. The number of GTPase-mediated signalling pathways that have been fully mapped from a specific receptor to a specific final target is rather low.

With this Special Issue, we would like to encourage the publication of further details about the signalling function of plant G-proteins. Manuscripts characterising the G-proteins themselves, as well as their regulators, effectors and further upstream and downstream events linking these molecules to developmental, hormonal, and environmental responses, are welcome.

Prof. Dr. Attila Fehér
Guest Editor

Manuscript Submission Information

Manuscripts should be submitted online at www.mdpi.com by registering and logging in to this website. Once you are registered, click here to go to the submission form. Manuscripts can be submitted until the deadline. All submissions that pass pre-check are peer-reviewed. Accepted papers will be published continuously in the journal (as soon as accepted) and will be listed together on the special issue website. Research articles, review articles as well as short communications are invited. For planned papers, a title and short abstract (about 100 words) can be sent to the Editorial Office for announcement on this website.

Submitted manuscripts should not have been published previously, nor be under consideration for publication elsewhere (except conference proceedings papers). All manuscripts are thoroughly refereed through a single-blind peer-review process. A guide for authors and other relevant information for submission of manuscripts is available on the Instructions for Authors page. Plants is an international peer-reviewed open access semimonthly journal published by MDPI.

Please visit the Instructions for Authors page before submitting a manuscript. The Article Processing Charge (APC) for publication in this open access journal is 2700 CHF (Swiss Francs). Submitted papers should be well formatted and use good English. Authors may use MDPI's English editing service prior to publication or during author revisions.

Keywords

  • GTP-binding
  • GTPase
  • effector
  • heterotrimeric GTP-binding protein
  • RAB GTPase
  • ROP GTPase
  • ARF GTPase
  • small GTP-binding proteins
  • signal transduction
  • guanine nucleotide exchange factor (GEF)
  • GTPase accelerator protein (GAP)
  • guanine nucleotide dissociation inhibitor (GDI)
  • cell polarity
  • cytoskeleton
  • protein kinase
  • plant morphogenesis
  • hormonal signalling
  • plant defence
  • abiotic stress tolerance
  • vesicular transport

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Published Papers (3 papers)

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Research

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8 pages, 2704 KiB  
Communication
OsGGC2, Gγ Subunit of Heterotrimeric G Protein, Regulates Plant Height by Functionally Overlapping with DEP1 in Rice
by Genki Chaya, Shuhei Segami, Moeka Fujita, Yoichi Morinaka, Yukimoto Iwasaki and Kotaro Miura
Plants 2022, 11(3), 422; https://doi.org/10.3390/plants11030422 - 3 Feb 2022
Cited by 7 | Viewed by 2283
Abstract
Plant heterotrimeric G proteins have been shown to regulate the size of various organs. There are three types of Gγ subunits in plants: type A, consisting of a canonical Gγ domain; type B, possessing a plant-specific domain at the N-terminus of the Gγ [...] Read more.
Plant heterotrimeric G proteins have been shown to regulate the size of various organs. There are three types of Gγ subunits in plants: type A, consisting of a canonical Gγ domain; type B, possessing a plant-specific domain at the N-terminus of the Gγ domain; and type C, possessing a plant-specific domain at the C-terminal of the Gγ domain. There is one type A, one type B, and three type C of the five γ-subunits in the rice genome. In type C Gγ subunits, GS3, which controls grain size; DEP1, which controls plant height and panicle branching; and their homolog OsGGC2, which affects grain size, have been reported; however, the function of each gene, their interactions, and molecular mechanisms for the control of plant height have not yet been clarified. In this study, we generated loss-of-function mutants of DEP1 and OsGGC2, which have high homology and similar expression, and investigated their phenotypes. Since both dep1 and osggc2 mutants were dwarfed and the double mutants showed a synergistic phenotype, we concluded that both DEP1 and OsGGC2 are positive regulators of plant height and that their functions are redundant. Full article
(This article belongs to the Special Issue The Signalling Function of Plant GTP-Binding Proteins)
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15 pages, 4243 KiB  
Article
The Arabidopsis Rho of Plants GTPase ROP1 Is a Potential Calcium-Dependent Protein Kinase (CDPK) Substrate
by Dalma Ménesi, Éva Klement, Györgyi Ferenc and Attila Fehér
Plants 2021, 10(10), 2053; https://doi.org/10.3390/plants10102053 - 29 Sep 2021
Cited by 7 | Viewed by 3213
Abstract
Plant Rho-type GTPases (ROPs) are versatile molecular switches involved in a number of signal transduction pathways. Although it is well known that they are indirectly linked to protein kinases, our knowledge about their direct functional interaction with upstream or downstream protein kinases is [...] Read more.
Plant Rho-type GTPases (ROPs) are versatile molecular switches involved in a number of signal transduction pathways. Although it is well known that they are indirectly linked to protein kinases, our knowledge about their direct functional interaction with upstream or downstream protein kinases is scarce. It is reasonable to suppose that similarly to their animal counterparts, ROPs might also be regulated by phosphorylation. There is only, however, very limited experimental evidence to support this view. Here, we present the analysis of two potential phosphorylation sites of AtROP1 and two types of potential ROP-kinases. The S74 site of AtROP1 has been previously shown to potentially regulate AtROP1 activation dependent on its phosphorylation state. However, the kinase phosphorylating this evolutionarily conserved site could not be identified: we show here that despite of the appropriate phosphorylation site consensus sequences around S74 neither the selected AGC nor CPK kinases phosphorylate S74 of AtROP1 in vitro. However, we identified several phosphorylation sites other than S74 for the CPK17 and 34 kinases in AtROP1. One of these sites, S97, was tested for biological relevance. Although the mutation of S97 to alanine (which cannot be phosphorylated) or glutamic acid (which mimics phosphorylation) somewhat altered the protein interaction strength of AtROP1 in yeast cells, the mutant proteins did not modify pollen tube growth in an in vivo test. Full article
(This article belongs to the Special Issue The Signalling Function of Plant GTP-Binding Proteins)
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Review

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17 pages, 636 KiB  
Review
Heterotrimeric G Protein Signaling in Abiotic Stress
by Yijie Wang and Jose Ramón Botella
Plants 2022, 11(7), 876; https://doi.org/10.3390/plants11070876 - 25 Mar 2022
Cited by 13 | Viewed by 3791
Abstract
As sessile organisms, plants exhibit extraordinary plasticity and have evolved sophisticated mechanisms to adapt and mitigate the adverse effects of environmental fluctuations. Heterotrimeric G proteins (G proteins), composed of α, β, and γ subunits, are universal signaling molecules mediating the response to a [...] Read more.
As sessile organisms, plants exhibit extraordinary plasticity and have evolved sophisticated mechanisms to adapt and mitigate the adverse effects of environmental fluctuations. Heterotrimeric G proteins (G proteins), composed of α, β, and γ subunits, are universal signaling molecules mediating the response to a myriad of internal and external signals. Numerous studies have identified G proteins as essential components of the organismal response to stress, leading to adaptation and ultimately survival in plants and animal systems. In plants, G proteins control multiple signaling pathways regulating the response to drought, salt, cold, and heat stresses. G proteins signal through two functional modules, the Gα subunit and the Gβγ dimer, each of which can start either independent or interdependent signaling pathways. Improving the understanding of the role of G proteins in stress reactions can lead to the development of more resilient crops through traditional breeding or biotechnological methods, ensuring global food security. In this review, we summarize and discuss the current knowledge on the roles of the different G protein subunits in response to abiotic stress and suggest future directions for research. Full article
(This article belongs to the Special Issue The Signalling Function of Plant GTP-Binding Proteins)
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