Evidence map›Paper›PMID 19589775›Full record

ArticleThe Journal of biological chemistry2009

Subcomplexes of PA700, the 19 S regulator of the 26 S proteasome, reveal relative roles of AAA subunits in 26 S proteasome assembly and activation and ATPase activity.

David Thompson, Kevin Hakala, George N DeMartino

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.6field-weighted citation impact, top 6% 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

44 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Plasticity in the structure and assembly of proteasomes.The Journal of biological chemistry · 2026
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Proteasome Structure and Assembly.Journal of molecular biology · 2017
    Review
  10. Article
  11. 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
  12. Article
  13. An atomic structure of the human 26S proteasome.Nature structural & molecular biology · 2016
    Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Proteasome assembly.Cellular and molecular life sciences : CMLS · 2014
    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

3 authors at 1 institution in 1 country.

David ThompsonDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9040, USA.
Kevin Hakala
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

We have identified, purified, and characterized three subcomplexes of PA700, the 19 S regulatory complex of the 26 S proteasome. These subcomplexes (denoted PS-1, PS-2, and PS-3) collectively account for all subunits present in purified PA700 but contain no overlapping components or significant levels of non-PA700 proteins. Each subcomplex contained two of the six AAA subunits (Rpt1-6) that form the binding interface of PA700 with the 20 S proteasome, the protease component of the 26 S proteasome. Unlike intact PA700, no individual PA700 subcomplex displayed ATPase activity or proteasome activating activity. However, both activities were manifested by ATP-dependent in vitro reconstitution of PA700 from the subcomplexes. We exploited functional reconstitution to define and distinguish roles of different PA700 subunits in PA700 function by selective alteration of subunits within individual subcomplexes prior to reconstitution. Carboxypeptidase treatment of either PS-2 or PS-3, subcomplexes containing specific Rpt subunits previously shown to have important roles in 26 S proteasome assembly and activation, inhibited these processes but did not affect PA700 reconstitution or ATPase activity. Thus, the intact C termini of both subunits are required for 26 S proteasome assembly and activation but not for PA700 reconstitution. Surprisingly, carboxypeptidase treatment of PS-1 also inhibited 26 S proteasome assembly and activation upon reconstitution with untreated PS-2 and PS-3. These results suggest a previously unidentified role for other PA700 subunits in 26 S proteasome assembly and activation. Our results reveal relative structural and functional relationships among the AAA subunits of PA700 and new insights about mechanisms of 26 S proteasome assembly and activation.

Indexed as

Adenosine TriphosphatasesAdenosine TriphosphateAnimalsCattleElectrophoresis, Polyacrylamide GelErythrocytesGlycerolMass SpectrometryModels, BiologicalProteasome Endopeptidase ComplexProtein BindingProtein Structure, TertiarySubstrate SpecificityAdenosine TriphosphatasesAdenosine TriphosphateATP dependent 26S proteaseGlycerolPA700 proteasome activatorProteasome Endopeptidase Complex

Identifiers

PMID19589775
PMCPMC2757192
OpenAlexW2103672763

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.