Evidence map›Paper›PMID 19451657›Full record

ArticleThe Journal of biological chemistry2009

Farnesylation of pex19p is required for its structural integrity and function in peroxisome biogenesis.

Robert Rucktäschel, Sven Thoms, Vadim Sidorovitch, Andre Halbach, Markos Pechlivanis, Rudolf Volkmer, Kirill Alexandrov, Jürgen Kuhlmann, Hanspeter Rottensteiner, Ralf Erdmann

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

29 citing papers in PubMed, 54 citations in OpenAlex.

  1. Building peroxisomes: perspectives on plant peroxins.Biochemical Society transactions · 2026
    Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Review
  15. NaPi-IIa interacting partners and their (un)known functional roles.Pflugers Archiv : European journal of physiology · 2019
    Review
  16. Establishing the lipid droplet proteome: Mechanisms of lipid droplet protein targeting and degradation.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017
    Review
  17. Article
  18. Article
  19. Pex35 is a regulator of peroxisome abundance.Journal of cell science · 2017
    Article
  20. 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

10 authors at 4 institutions in 1 country.

Robert RucktäschelDepartment for Systems Biochemistry, Institute for Physiological Chemistry, University of Bochum, Universitätsstrasse 150, 44780 Bochum.
Sven Thoms
Vadim Sidorovitch
Andre Halbach
Markos Pechlivanis
Rudolf Volkmer
Kirill Alexandrov
Jürgen Kuhlmann
Hanspeter Rottensteiner
Ralf Erdmann
Ruhr University Bochum · DEMax Planck Institute of Molecular Physiology · DEMax Planck Society · DECharité - Universitätsmedizin Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The conserved CaaX box peroxin Pex19p is known to be modified by farnesylation. The possible involvement of this lipid modification in peroxisome biogenesis, the degree to which Pex19p is farnesylated, and its molecular function are unknown or controversial. We resolve these issues by first showing that the complete pool of Pex19p is processed by farnesyltransferase in vivo and that this modification is independent of peroxisome induction or the Pex19p membrane anchor Pex3p. Furthermore, genomic mutations of PEX19 prove that farnesylation is essential for proper matrix protein import into peroxisomes, which is supposed to be caused indirectly by a defect in peroxisomal membrane protein (PMP) targeting or stability. This assumption is corroborated by the observation that mutants defective in Pex19p farnesylation are characterized by a significantly reduced steady-state concentration of prominent PMPs (Pex11p, Ant1p) but also of essential components of the peroxisomal import machinery, especially the RING peroxins, which were almost depleted from the importomer. In vivo and in vitro, PMP recognition is only efficient when Pex19p is farnesylated with affinities differing by a factor of 10 between the non-modified and wild-type forms of Pex19p. Farnesylation is likely to induce a conformational change in Pex19p. Thus, isoprenylation of Pex19p contributes to substrate membrane protein recognition for the topogenesis of PMPs, and our results highlight the importance of lipid modifications in protein-protein interactions.

Indexed as

PrenylationAmino Acid MotifsCircular DichroismFarnesyltranstransferaseMembrane ProteinsMutationPeroxinsPeroxisomesProtein BindingProtein Sorting SignalsProtein StabilityProtein Structure, SecondaryProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsStructure-Activity RelationshipFarnesyltranstransferaseMembrane ProteinsPeroxinsPEX19 protein, S cerevisiaePEX3 protein, S cerevisiaeProtein Sorting SignalsSaccharomyces cerevisiae Proteins

Identifiers

PMID19451657
PMCPMC2742854
OpenAlexW2036885100

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.