Evidence map›Paper›PMID 24770418›Full record

ArticleThe Journal of biological chemistry2014

Molecular and cellular roles of PI31 (PSMF1) protein in regulation of proteasome function.

Xiaohua Li, David Thompson, Brajesh Kumar, George N DeMartino

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
2.8field-weighted citation impact, top 9% 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

38 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
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  12. Yeast PI31 inhibits the proteasome by a direct multisite mechanism.Nature structural & molecular biology · 2022
    Article
  13. Proteasome complexes experience profound structural and functional rearrangements throughout mammalian spermatogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  14. Article
  15. Review
  16. Article
  17. The proteasome regulator PI31 is required for protein homeostasis, synapse maintenance, and neuronal survival in mice.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  18. Article
  19. Article
  20. A Conserved Requirement forFrontiers in physiology · 2019
    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.

Xiaohua LiFrom the Department of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
David ThompsonFrom the Department of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
Brajesh KumarFrom the Department of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390.
George N DeMartinoFrom the Department of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390 george.demartino@utsouthwestern.edu.
The University of Texas Southwestern Medical Center · US

Funding

FUNCTION AND REGULATION OF THE PROTEASOMER01DK046181 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI DEMARTINO, GEORGE N. · 1994 to 2012
$3.2M
Function and regulation of the proteasomeR56DK046181 · NIDDK · UT SOUTHWESTERN MEDICAL CENTER · PI DEMARTINO, GEORGE N. · 2007 to 2007
$353k
NIDDK NIH HHS R01 DK046181NIDDK NIH HHS R56 DK046181
6 · The paper itself

Abstract

We investigated molecular features and cellular roles of PI31 (PSMF1) on regulation of proteasome function. PI31 has a C-terminal HbYX (where Hb is a hydrophobic amino acid, Y is tyrosine, and X is any amino acid) motif characteristic of several proteasome activators. Peptides corresponding to the PI31 C terminus also bind to and activate the 20 S proteasome in an HbYX-dependent manner, but intact PI31protein inhibits in vitro 20 S activity. Binding to and inhibition of the proteasome by PI31 are conferred by the HbYX-containing proline-rich C-terminal domain but do not require HbYX residues. Thus, multiple regions of PI31 bind independently to the proteasome and collectively determine effects on activity. PI31 blocks the ATP-dependent in vitro assembly of 26 S proteasome from 20 S proteasome and PA700 subcomplexes but has no effect on in vitro activity of the intact 26 S proteasome. To determine the physiologic significance of these in vitro effects, we assessed multiple aspects of cellular proteasome content and function after altering PI31 levels. We detected no change in overall cellular proteasome content or function when PI31 levels were either increased by moderate ectopic overexpression or decreased by RNA interference (RNAi). We also failed to identify a role of PI31 ADP-ribosylation as a mechanism for regulation of overall 26 S proteasome content and function, as recently proposed. Thus, despite its in vitro effects on various proteasome activities and its structural relationship to established proteasome regulators, cellular roles and mechanisms of PI31 in regulation of proteasome function remain unclear and require future definition.

Indexed as

Amino Acid MotifsAnimalsDrosophila melanogasterHEK293 CellsHeLa CellsHumansProteasome Endopeptidase ComplexProteinsProtein Structure, TertiaryATP dependent 26S proteaseProteasome Endopeptidase ComplexProteinsPSMF1 protein, humanHbYX MotifPI31Protease InhibitorProteasomeProtein ComplexProtein DegradationUbiquitin-dependent Protease

Identifiers

PMID24770418
PMCPMC4067172
OpenAlexW1999188297

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.