Evidence map›Paper›PMID 35741050›Full record

ReviewCells2022

Fission Impossible (?)-New Insights into Disorders of Peroxisome Dynamics.

Ruth E Carmichael, Markus Islinger, Michael Schrader

Open access · goldAbstract readReview
In one paragraph

Review in Cells, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.2field-weighted citation impact, top 22% 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

11 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Mammalian pexophagy at a glance.Journal of cell science · 2024
    Review
  8. The peroxisome: an update on mysteries 3.0.Histochemistry and cell biology · 2024
    Review
  9. Article
  10. Article
  11. 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

3 authors at 2 institutions in 2 countries.

Ruth E CarmichaelCollege of Life and Environmental Sciences, Biosciences, University of Exeter, Exeter EX4 4QD, UK.ORCID 0000-0003-2665-2966
Markus IslingerInstitute of Neuroanatomy, Mannheim Centre for Translational Neuroscience, Medical Faculty Mannheim, University of Heidelberg, 68167 Mannheim, Germany.ORCID 0000-0001-8881-0902
Michael SchraderCollege of Life and Environmental Sciences, Biosciences, University of Exeter, Exeter EX4 4QD, UK.ORCID 0000-0003-2146-0535
University of Exeter · GBHeidelberg University · DE

Funding

Biotechnology and Biological Sciences Research Council BB/R016844/1Biotechnology and Biological Sciences Research Council BB/T002255/1
6 · The paper itself

Abstract

Peroxisomes are highly dynamic and responsive organelles, which can adjust their morphology, number, intracellular position, and metabolic functions according to cellular needs. Peroxisome multiplication in mammalian cells involves the concerted action of the membrane-shaping protein PEX11β and division proteins, such as the membrane adaptors FIS1 and MFF, which recruit the fission GTPase DRP1 to the peroxisomal membrane. The latter proteins are also involved in mitochondrial division. Patients with loss of DRP1, MFF or PEX11β function have been identified, showing abnormalities in peroxisomal (and, for the shared proteins, mitochondrial) dynamics as well as developmental and neurological defects, whereas the metabolic functions of the organelles are often unaffected. Here, we provide a timely update on peroxisomal membrane dynamics with a particular focus on peroxisome formation by membrane growth and division. We address the function of PEX11β in these processes, as well as the role of peroxisome-ER contacts in lipid transfer for peroxisomal membrane expansion. Furthermore, we summarize the clinical phenotypes and pathophysiology of patients with defects in the key division proteins DRP1, MFF, and PEX11β as well as in the peroxisome-ER tether ACBD5. Potential therapeutic strategies for these rare disorders with limited treatment options are discussed.

Indexed as

Mitochondrial ProteinsPeroxisomesAnimalsGTP PhosphohydrolasesHumansMammalsMembrane ProteinsMitochondriaMitochondrial DynamicsGTP PhosphohydrolasesMembrane ProteinsMitochondrial ProteinsACBD5division defectsdynamin-related protein 1FIS1membrane fissionmitochondriamitochondrial fission factororganelle dynamicsperoxisomesPEX11β

Identifiers

PMID35741050
PMCPMC9221819
OpenAlexW4282928025

What Socratic holds

Textmetadata
LicenceCC BY
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 Socratic graph.