Evidence map›Paper›PMID 29934401›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

PIP30/FAM192A is a novel regulator of the nuclear proteasome activator PA28γ.

Beata Jonik-Nowak, Thomas Menneteau, Didier Fesquet, Véronique Baldin, Catherine Bonne-Andrea, Francisca Méchali, Bertrand Fabre, Prisca Boisguerin, Sylvain de Rossi, Corinne Henriquet and 8 more

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.9field-weighted citation impact, top 14% 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

23 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. REGγ is essential to maintain bone homeostasis by degrading TRAF6, preventing osteoporosis.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  7. Article
  8. Review
  9. Coilin and Cajal bodies.Nucleus (Austin, Tex.) · 2023
    Review
  10. Article
  11. Review
  12. Article
  13. Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. PA28γ, an Accomplice to Malignant Cancer.Frontiers in oncology · 2020
    Review
  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

18 authors at 3 institutions in 2 countries.

Beata Jonik-NowakCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), Université de Montpellier, CNRS, 34090 Montpellier, France.
Thomas MenneteauInstitut de Pharmacologie et Biologie Structurale (IPBS), CNRS, Université de Toulouse-Université Paul Sabatier, 31062 Toulouse, France.
Didier FesquetCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), Université de Montpellier, CNRS, 34090 Montpellier, France.ORCID 0000-0001-5657-9689
Véronique BaldinCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), Université de Montpellier, CNRS, 34090 Montpellier, France.ORCID 0000-0001-8523-0494
Catherine Bonne-AndreaCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), Université de Montpellier, CNRS, 34090 Montpellier, France.
Francisca MéchaliCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), Université de Montpellier, CNRS, 34090 Montpellier, France.
Bertrand FabreInstitut de Pharmacologie et Biologie Structurale (IPBS), CNRS, Université de Toulouse-Université Paul Sabatier, 31062 Toulouse, France.
Prisca BoisguerinCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), Université de Montpellier, CNRS, 34090 Montpellier, France.
Sylvain de RossiMontpellier Ressources Imagerie (MRI) Facility, Biocampus UMS3426, CNRS, 34090 Montpellier, France.
Corinne HenriquetInstitut de Recherche en Cancérologie de Montpellier (IRCM) - INSERM U1194, Institut Régional du Cancer de Montpellier, Université de Montpellier, F-34298 Montpellier, France.
Martine PugnièreInstitut de Recherche en Cancérologie de Montpellier (IRCM) - INSERM U1194, Institut Régional du Cancer de Montpellier, Université de Montpellier, F-34298 Montpellier, France.
Manuelle Ducoux-PetitInstitut de Pharmacologie et Biologie Structurale (IPBS), CNRS, Université de Toulouse-Université Paul Sabatier, 31062 Toulouse, France.
Odile Burlet-SchiltzInstitut de Pharmacologie et Biologie Structurale (IPBS), CNRS, Université de Toulouse-Université Paul Sabatier, 31062 Toulouse, France.
Angus I LamondCentre for Gene Regulation and Expression, School of Life Sciences, DD1 5HL Dundee, United Kingdom.
Philippe FortCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), Université de Montpellier, CNRS, 34090 Montpellier, France.
Séverine BoulonCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), Université de Montpellier, CNRS, 34090 Montpellier, France; severine.boulon@crbm.cnrs.fr Marie-Pierre.Bousquet@ipbs.fr olivier.coux@crbm.cnrs.fr.
Marie-Pierre BousquetInstitut de Pharmacologie et Biologie Structurale (IPBS), CNRS, Université de Toulouse-Université Paul Sabatier, 31062 Toulouse, France; severine.boulon@crbm.cnrs.fr Marie-Pierre.Bousquet@ipbs.fr olivier.coux@crbm.cnrs.fr.
Olivier CouxCentre de Recherche en Biologie Cellulaire de Montpellier (CRBM), Université de Montpellier, CNRS, 34090 Montpellier, France; severine.boulon@crbm.cnrs.fr Marie-Pierre.Bousquet@ipbs.fr olivier.coux@crbm.cnrs.fr.ORCID 0000-0001-8455-3849
Centre National de la Recherche Scientifique · FRInserm · FRUniversity of Dundee · GB

Funding

Wellcome TrustWellcome Trust 097945/B/11/ZWellcome Trust 108058/Z/15/Z
6 · The paper itself

Abstract

PA28γ is a nuclear activator of the 20S proteasome involved in the regulation of several essential cellular processes, such as cell proliferation, apoptosis, nuclear dynamics, and cellular stress response. Unlike the 19S regulator of the proteasome, which specifically recognizes ubiquitylated proteins, PA28γ promotes the degradation of several substrates by the proteasome in an ATP- and ubiquitin-independent manner. However, its exact mechanisms of action are unclear and likely involve additional partners that remain to be identified. Here we report the identification of a cofactor of PA28γ, PIP30/FAM192A. PIP30 binds directly and specifically via its C-terminal end and in an interaction stabilized by casein kinase 2 phosphorylation to both free and 20S proteasome-associated PA28γ. Its recruitment to proteasome-containing complexes depends on PA28γ and its expression increases the association of PA28γ with the 20S proteasome in cells. Further dissection of its possible roles shows that PIP30 alters PA28γ-dependent activation of peptide degradation by the 20S proteasome in vitro and negatively controls in cells the presence of PA28γ in Cajal bodies by inhibition of its association with the key Cajal body component coilin. Taken together, our data show that PIP30 deeply affects PA28γ interactions with cellular proteins, including the 20S proteasome, demonstrating that it is an important regulator of PA28γ in cells and thus a new player in the control of the multiple functions of the proteasome within the nucleus.

Indexed as

AutoantigensCell NucleusHeLa CellsHumansNuclear ProteinsProteasome Endopeptidase ComplexProtein BindingProtein DomainsProteinsAutoantigensFAM193A protein, humanKi antigenNuclear Proteinsp80-coilinProteasome Endopeptidase ComplexProteinsCajal bodiesFAM192Anuclear proteolysisPA28γproteasome

Identifiers

PMID29934401
PMCPMC6048556
OpenAlexW2809161673

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.