Evidence map›Paper›PMID 8858168›Full record

ArticleThe Journal of cell biology1996

Redox-sensitive homodimerization of Pex11p: a proposed mechanism to regulate peroxisomal division.

P A Marshall, J M Dyer, M E Quick, J M Goodman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
1.5field-weighted citation impact, top 18% 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

43 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Methods to Analyze the Redox Reactivity of Plant Proteins.Methods in molecular biology (Clifton, N.J.) · 2022
    Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Peroxisomes take shape.Nature reviews. Molecular cell biology · 2013
    Review
  16. Article
  17. Article
  18. The peroxisome: an update on mysteries.Histochemistry and cell biology · 2012
    Review
  19. Article
  20. Article
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.

P A MarshallDepartment of Pharmacology, University of Texas Southwestern Medical Center, Dallas 75235-9041, USA.
J M Dyer
M E Quick
J M Goodman
The University of Texas Southwestern Medical Center · US

Funding

MECHANISMS OF DRUG ACTION AND DISPOSITIONT32GM007062 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI MANGELSDORF, DAVID J · 1985 to 2020
$7.4M
INDUCTION OF AN ORGANELLE: THE YEAST PEROXISOMER01GM031859 · NIGMS · UNIVERSITY OF TEXAS SW MED CTR/DALLAS · PI GOODMAN, JOEL M · 1985 to 1999
–
NIGMS NIH HHS GM 16974NIGMS NIH HHS GM 31859NIGMS NIH HHS T32 GM-07062
6 · The paper itself

Abstract

Pex11p (formerly Pmp27) has been implicated in peroxisomal proliferation (Erdmann, R., and G. Blobel. 1995. J. Cell Biol. 128; 509-523; Marshall, P.A., Y.I. Krimkevich, R.H. Lark, J.M. Dyer, M. Veenhuis, and J.M. Goodman, 1995. J. Cell Biol. 129; 345-355). In its absence, peroxisomes in Saccharomyces cerevisiae fail to proliferate in response to oleic acid; instead, one or two large peroxisomes are formed. Conversely, overproduction of Pex11p causes an increase in peroxisomal number. In this report, we confirm the function of Pex11p in organelle proliferation by demonstrating that this protein can cause fragmentation in vivo of large peroxisomes into smaller organelles. Pex11p is on the inner surface of the peroxisomal membrane. It can form homodimers, and this species is more abundant in mature peroxisomes than in proliferating organelles. Removing one of the three cysteines in the protein inhibits homodimerization. This cysteine 3-->alanine mutation leads to an increase in number and a decrease in peroxisomal density, compared with the wild-type protein, in response to oleic acid. We propose that the active species is the "monomeric" form, and that the increasing oxidative metabolism within maturing peroxisomes causes dimer formation and inhibition of further organelle division.

Indexed as

Saccharomyces cerevisiae ProteinsBase SequenceCell DivisionCross-Linking ReagentsCysteineDimerizationFungal ProteinsGalactoseIntracellular MembranesMembrane ProteinsMicrobodiesMolecular Sequence DataMolecular WeightOleic AcidOxidation-ReductionPeroxinsbis(sulfosuccinimidyl)suberateCross-Linking ReagentsCysteineFungal ProteinsGalactoseMembrane ProteinsOleic AcidPeroxinsPEX11 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSuccinimides

Identifiers

PMID8858168
PMCPMC2121026
OpenAlexW2009392934

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.