Evidence map›Paper›PMID 21628461›Full record

ArticleThe Journal of biological chemistry2011

C termini of proteasomal ATPases play nonequivalent roles in cellular assembly of mammalian 26 S proteasome.

Young-Chan Kim, George N DeMartino

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

27 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Proteasome Activation to Combat Proteotoxicity.Molecules (Basel, Switzerland) · 2019
    Review
  6. Aim for the core: suitability of the ubiquitin-independent 20S proteasome as a drug target in neurodegeneration.Translational research : the journal of laboratory and clinical medicine · 2018
    Review
  7. Article
  8. Article
  9. Nucleotide-dependent switch in proteasome assembly mediated by the Nas6 chaperone.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  10. Article
  11. Structural basis for dynamic regulation of the human 26S proteasome.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  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

2 authors at 1 institution in 1 country.

Young-Chan KimDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9040, USA.
George N DeMartino
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
NIDDK NIH HHS R01 DK046181NIDDK NIH HHS R01 DK46181
6 · The paper itself

Abstract

The 26 S proteasome comprises two multisubunit subcomplexes as follows: 20 S proteasome and PA700/19 S regulatory particle. The cellular mechanisms by which these subcomplexes assemble into 26 S proteasome and the molecular determinants that govern the assembly process are poorly defined. Here, we demonstrate the nonequivalent roles of the C termini of six AAA subunits (Rpt1-Rpt6) of PA700 in 26 S proteasome assembly in mammalian cells. The C-terminal HbYX motif (where Hb is a hydrophobic residue, Y is tyrosine, and X is any amino acid) of each of two subunits, Rpt3 and Rpt5, but not that of a third subunit Rpt2, was essential for assembly of 26 S proteasome. The C termini of none of the three non-HbYX motif Rpt subunits were essential for cellular 26 S proteasome assembly, although deletion of the last three residues of Rpt6 destabilized the 20 S-PA700 interaction. Rpt subunits defective for assembly into 26 S proteasome due to C-terminal truncations were incorporated into intact PA700. Moreover, intact PA700 accumulated as an isolated subcomplex when cellular 20 S proteasome content was reduced by RNAi. These results indicate that 20 S proteasome is not an obligatory template for assembly of PA700. Collectively, these results identify specific structural elements of two Rpt subunits required for 26 S proteasome assembly, demonstrate that PA700 can be assembled independently of the 20 S proteasome, and suggest that intact PA700 is a direct intermediate in the cellular pathway of 26 S proteasome assembly.

Indexed as

Adenosine TriphosphatasesAmino Acid MotifsAmino Acid SequenceHEK293 CellsHumansProteasome Endopeptidase ComplexProtein Structure, TertiarySequence DeletionAdenosine TriphosphatasesATP dependent 26S proteasePA700 proteasome activatorProteasome Endopeptidase Complex

Identifiers

PMID21628461
PMCPMC3143629
OpenAlexW2011313101

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.