Evidence map›Paper›PMID 32854114›Full record

ArticleThe Journal of cell biology2020

Mitotic phosphorylation of Pex14p regulates peroxisomal import machinery.

Koichiro Yamashita, Shigehiko Tamura, Masanori Honsho, Hiroto Yada, Yuichi Yagita, Hidetaka Kosako, Yukio Fujiki

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

15 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Review
  7. The peroxisome: an update on mysteries 3.0.Histochemistry and cell biology · 2024
    Review
  8. Review
  9. Article
  10. Analysis of Peroxisome Biogenesis by Phos-Tag SDS-PAGE.Methods in molecular biology (Clifton, N.J.) · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. 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

7 authors at 2 institutions in 1 country.

Koichiro YamashitaGraduate School of Systems Life Sciences, Kyushu University, Fukuoka, Japan.
Shigehiko TamuraFaculty of Arts and Science, Kyushu University, Fukuoka, Japan.
Masanori HonshoDivision of Organelle Homeostasis, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Hiroto YadaGraduate School of Systems Life Sciences, Kyushu University, Fukuoka, Japan.
Yuichi YagitaDivision of Organelle Homeostasis, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Hidetaka KosakoDivision of Cell Signaling, Fujii Memorial Institute of Medical Sciences, Tokushima University, Tokushima, Japan.
Yukio FujikiDivision of Organelle Homeostasis, Medical Institute of Bioregulation, Kyushu University, Fukuoka, Japan.
Kyushu University · JPTokushima University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peroxisomal matrix proteins are imported into peroxisomes via membrane-bound docking/translocation machinery. One central component of this machinery is Pex14p, a peroxisomal membrane protein involved in the docking of Pex5p, the receptor for peroxisome targeting signal type 1 (PTS1). Studies in several yeast species have shown that Pex14p is phosphorylated in vivo, whereas no function has been assigned to Pex14p phosphorylation in yeast and mammalian cells. Here, we investigated peroxisomal protein import and its dynamics in mitotic mammalian cells. In mitotically arrested cells, Pex14p is phosphorylated at Ser-232, resulting in a lower import efficiency of catalase, but not the majority of proteins including canonical PTS1 proteins. Conformational change induced by the mitotic phosphorylation of Pex14p more likely increases homomeric interacting affinity and suppresses topological change of its N-terminal part, thereby giving rise to the retardation of Pex5p export in mitotic cells. Taken together, these data show that mitotic phosphorylation of Pex14p and consequent suppression of catalase import are a mechanism of protecting DNA upon nuclear envelope breakdown at mitosis.

Indexed as

Amino Acid SequenceAnimalsCatalaseCHO CellsCricetinaeCricetulusHeLa CellsHumansMembrane ProteinsMitosisPeroxisomesPeroxisome-Targeting Signal 1 ReceptorPhosphorylationProtein BindingProtein TransportRepressor ProteinsCatalaseMembrane ProteinsPeroxisome-Targeting Signal 1 ReceptorPEX14 protein, humanRepressor Proteins

Identifiers

PMID32854114
PMCPMC7659713
OpenAlexW3080168134

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.