Evidence map›Paper›PMID 17220359›Full record

ArticlePlant physiology2007

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

Qin Zeng, Xuejun Wang, Mark P Running

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.8field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

36 citing papers in PubMed, 84 citations in OpenAlex.

  1. Review
  2. Review
  3. Global analysis of membrane protein S-acylation in the model plantbioRxiv : the preprint server for biology · 2025
    Article
  4. Review
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  7. Review
  8. Article
  9. Article
  10. Dynamic Protein S-Acylation in Plants.International journal of molecular sciences · 2019
    Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Qin ZengDonald Danforth Plant Science Center, St. Louis, Missouri 63132, USA.
Xuejun Wang
Mark P Running
Donald Danforth Plant Science Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

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 yellow fluorescent protein-fused AGG1 and AGG2 are associated with plasma membranes, with AGG1 associated with internal membranes as well. Both can be prenylated by either protein geranylgeranyltransferase I (PGGT-I) or protein farnesyltransferase (PFT). Their membrane localization is intact in mutants lacking PFT activity and largely intact in mutants lacking PGGT-I activity but is disrupted in mutants lacking both PFT and PGGT-I activity. Unlike in mammals, Arabidopsis Ggammas do not rely on functional Galpha for membrane targeting. Mutation of the sixth to last cysteine, the putative S-acylation acceptor site, causes a dramatic change in AGG2 but not AGG1 localization pattern, suggesting S-acylation serves as an important additional signal for AGG2 to be targeted to the plasma membrane. Domain-swapping experiments suggest that a short charged sequence at the AGG2 C terminus contributes to AGG2's efficient membrane targeting compared to AGG1. Our data show the large degree to which PFT and PGGT-I can compensate for each other in plants and suggest that differential lipid modification plays an important regulatory role in plant protein localization.

Indexed as

AcylationAmino Acid SequenceArabidopsisArabidopsis ProteinsGTP-Binding Protein alpha SubunitsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma SubunitsMolecular Sequence DataMutationProtein PrenylationProtein TransportSequence AlignmentAGB1 protein, ArabidopsisAGG1 protein, ArabidopsisAGG2 protein, ArabidopsisArabidopsis ProteinsGPA1 protein, ArabidopsisGTP-Binding Protein alpha SubunitsGTP-Binding Protein beta SubunitsGTP-Binding Protein gamma Subunits

Identifiers

PMID17220359
PMCPMC1820929
OpenAlexW2127029088

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.