Evidence map›Paper›PMID 18641086›Full record

ArticlePlant physiology2008

Functional analysis of Arabidopsis postprenylation CaaX processing enzymes and their function in subcellular protein targeting.

Keren Bracha-Drori, Keren Shichrur, Tsofnat Cohen Lubetzky, Shaul Yalovsky

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

38 citing papers in PubMed, 57 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Drought and Oxidative Stress in Flax (Antioxidants (Basel, Switzerland) · 2023
    Article
  12. Article
  13. Genomic analysis for heat and combined heat-drought resilience in bread wheat under field conditions.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2022
    Article
  14. Article
  15. Article
  16. Article
  17. Protein Prenylation in Plant Stress Responses.Molecules (Basel, Switzerland) · 2019
    Review
  18. Rho-of-plant activated root hair formation requiresDevelopment (Cambridge, England) · 2019
    Article
  19. Review
  20. Rce1: mechanism and inhibition.Critical reviews in biochemistry and molecular biology · 2018
    Review
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

4 authors at 1 institution in 1 country.

Keren Bracha-DroriDepartment of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel.
Keren Shichrur
Tsofnat Cohen Lubetzky
Shaul Yalovsky
Tel Aviv University · IL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Prenylation is a posttranslational protein modification essential for developmental processes and response to abscisic acid. Following prenylation, the three C-terminal residues are proteoliticaly removed and in turn the free carboxyl group of the isoprenyl cysteine is methylated. The proteolysis and methylation, collectively referred to as CaaX processing, are catalyzed by Ste24 endoprotease or Rce1 endoprotease and by an isoprenyl cysteine methyltransferase (ICMT). Arabidopsis (Arabidopsis thaliana) contains single STE24 and RCE1 and two ICMT homologs. Here we show that in yeast (Saccharomyces cerevisiae) AtRCE1 promoted a-mating factor secretion and membrane localization of a ROP GTPase. Furthermore, green fluorescent protein fusion proteins of AtSTE24, AtRCE1, AtICMTA, and AtICMTB are colocalized in the endoplasmic reticulum, indicating that prenylated proteins reach this compartment and that CaaX processing is likely required for subcellular targeting. AtICMTB can process yeast a-factor more efficiently than AtICMTA. Sequence and mutational analyses revealed that the higher activity AtICMTB is conferred by five residues, which are conserved between yeast Ste14p, human ICMT, and AtICMTB but not in AtICMTA. Quantitative real-time reverse transcription-polymerase chain reaction and microarray data show that AtICMTA expression is significantly lower compared to AtICMTB. AtICMTA null mutants have a wild-type phenotype, indicating that its function is redundant. However, AtICMT RNAi lines had fasciated inflorescence stems, altered phylotaxis, and developed multiple buds without stem elongation. The phenotype of the ICMT RNAi lines is similar to farnesyltransferase beta-subunit mutant enhanced response to abscisic acid2 but is more subtle. Collectively, the data suggest that AtICMTB is likely the major ICMT and that methylation modulates activity of prenylated proteins.

Indexed as

Amino Acid SequenceArabidopsisConserved SequenceDNA Mutational AnalysisEndoplasmic ReticulumGenetic Complementation TestLigasesMethylationMolecular Sequence DataMutagenesis, InsertionalPhenotypeProtein MethyltransferasesProtein TransportReverse Transcriptase Polymerase Chain ReactionRNA InterferenceYeastsLigasesProtein Methyltransferasesprotein-S-isoprenylcysteine O-methyltransferaseRCE1 protein, Arabidopsis

Identifiers

PMID18641086
PMCPMC2528099
OpenAlexW2030060634

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.