Heterotrimeric G Proteins in Plants: Canonical and Atypical Gα Subunits.
G protein activation
GDP-GTP exchange
GTPase
heterotrimeric G proteins
phosphorylation
plant biology
signal transduction
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
31 Oct 2021
31 Oct 2021
Historique:
received:
06
10
2021
revised:
26
10
2021
accepted:
27
10
2021
entrez:
13
11
2021
pubmed:
14
11
2021
medline:
17
12
2021
Statut:
epublish
Résumé
Heterotrimeric GTP-binding proteins (G proteins), consisting of Gα, Gβ and Gγ subunits, transduce signals from a diverse range of extracellular stimuli, resulting in the regulation of numerous cellular and physiological functions in Eukaryotes. According to the classic G protein paradigm established in animal models, the bound guanine nucleotide on a Gα subunit, either guanosine diphosphate (GDP) or guanosine triphosphate (GTP) determines the inactive or active mode, respectively. In plants, there are two types of Gα subunits: canonical Gα subunits structurally similar to their animal counterparts and unconventional extra-large Gα subunits (XLGs) containing a C-terminal domain homologous to the canonical Gα along with an extended N-terminal domain. Both Gα and XLG subunits interact with Gβγ dimers and regulator of G protein signalling (RGS) protein. Plant G proteins are implicated directly or indirectly in developmental processes, stress responses, and innate immunity. It is established that despite the substantial overall similarity between plant and animal Gα subunits, they convey signalling differently including the mechanism by which they are activated. This review emphasizes the unique characteristics of plant Gα subunits and speculates on their unique signalling mechanisms.
Identifiants
pubmed: 34769272
pii: ijms222111841
doi: 10.3390/ijms222111841
pmc: PMC8584482
pii:
doi:
Substances chimiques
GTP-Binding Protein alpha Subunits
0
Plant Proteins
0
Guanosine Diphosphate
146-91-8
Guanosine Triphosphate
86-01-1
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
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