Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Dual lipid modification of Arabidopsis Ggamma-subunits is required for efficient plasma membrane targeting.

Plant physiology - 1 Mar 2007

Zeng Qin, Wang Xuejun, Running Mark P

Abstract excerpt

Posttranslational lipid modifications are important for proper localization of many proteins in eukaryotic cells. However, the functional interrelationships between lipid modification processes in plants remain unclear. Here we demonstrate that the two heterotrimeric G-protein gamma-subunits from Arabidopsis (Arabidopsis thaliana), AGG1 and AGG2, are prenylated, and AGG2 is S-acylated. In wild type, enhanced...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Acylation
Share to Arabidopsis Proteins
Share to GTP-Binding Protein alpha Subunits

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to GTP-Binding Protein beta Subunits

Share to GTP-Binding Protein gamma Subunits

Share to Protein Prenylation

Share to Protein Transport

Share to Sequence Alignment

Source

Open in PubMed Open full text

Identifiers

PMID: 17220359
DOI: 10.1104/pp.106.093583
PMCID: PMC1820929

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Dual lipid modification of Arabidopsis Ggamma-subunits is required for efficient plasma membrane targeting.PMID 17220359Read ↗

Plant G protein heterotrimers require dual lipidation motifs of Galpha and Ggamma and do not dissociate upon activation.Semantic proximity Read ↗

Extra-Large G Proteins Expand the Repertoire of Subunits in Arabidopsis Heterotrimeric G Protein Signaling.Semantic proximity Read ↗

Heterotrimeric G protein subunits differentially respond to endoplasmic reticulum stress in Arabidopsis.Semantic proximity Read ↗

An atypical heterotrimeric G-protein γ-subunit is involved in guard cell K⁺-channel regulation and morphological development in Arabidopsis thaliana.Semantic proximity Read ↗

Ggamma1 + Ggamma2 not equal to Gbeta: heterotrimeric G protein Ggamma-deficient mutants do not recapitulate all phenotypes of Gbeta-deficient mutants.Semantic proximity Read ↗

Conversion of protein farnesyltransferase to a geranylgeranyltransferase.Semantic proximity Read ↗

Growth attenuation under saline stress is mediated by the heterotrimeric G protein complex.Semantic proximity Read ↗

Membrane-localized extra-large G proteins and Gbg of the heterotrimeric G proteins form functional complexes engaged in plant immunity in Arabidopsis.Semantic proximity Read ↗

The CaaX specificities of Arabidopsis protein prenyltransferases explain era1 and ggb phenotypes.Semantic proximity Read ↗

G protein-coupled receptor-type G proteins are required for light-dependent seedling growth and fertility in Arabidopsis.Semantic proximity Read ↗

Arabidopsis thaliana GPAT8 and GPAT9 are localized to the ER and possess distinct ER retrieval signals: functional divergence of the dilysine ER retrieval motif in plant cells.Semantic proximity Read ↗

The G Protein β-Subunit, AGB1, Interacts with FERONIA in RALF1-Regulated Stomatal Movement.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.