Evidence map›Paper›PMID 20937828›Full record

ArticleThe Journal of biological chemistry2010

The C terminus of Rpt3, an ATPase subunit of PA700 (19 S) regulatory complex, is essential for 26 S proteasome assembly but not for activation.

Brajesh Kumar, Young-Chan Kim, George N DeMartino

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.5field-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

24 citing papers in PubMed, 37 citations in OpenAlex.

  1. Review
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  11. Review
  12. 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
  13. Article
  14. Review
  15. Review
  16. Article
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  18. Bipartite determinants mediate an evolutionarily conserved interaction between Cdc48 and the 20S peptidase.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  19. Article
  20. Dual functions of the Hsm3 protein in chaperoning and scaffolding regulatory particle subunits during the proteasome assembly.Proceedings of the National Academy of Sciences of the United States of America · 2012
    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.

Brajesh KumarDepartment of Physiology, University of Texas Southwestern Medical Center, Dallas, Texas 75390-9040, USA.
Young-Chan Kim
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

PA700, the 19 S regulatory subcomplex of the 26 S proteasome, contains a heterohexameric ring of AAA subunits (Rpt1 to -6) that forms the binding interface with a heteroheptameric ring of α subunits (α1 to -7) of the 20 S proteasome. Binding of these subcomplexes is mediated by interactions of C termini of certain Rpt subunits with cognate binding sites on the 20 S proteasome. Binding of two Rpt subunits (Rpt2 and Rpt5) depends on their last three residues, which share an HbYX motif (where Hb is a hydrophobic amino acid) and open substrate access gates in the center of the α ring. The relative roles of other Rpt subunits for proteasome binding and activation remain poorly understood. Here we demonstrate that the C-terminal HbYX motif of Rpt3 binds to the 20 S proteasome but does not promote proteasome gating. Binding requires the last three residues and occurs at a dedicated site on the proteasome. A C-terminal peptide of Rpt3 blocked ATP-dependent in vitro assembly of 26 S proteasome from PA700 and 20 S proteasome. In HEK293 cells, wild-type Rpt3, but not Rpt3 lacking the HbYX motif was incorporated into 26 S proteasome. These results indicate that the C terminus of Rpt3 was required for cellular assembly of this subunit into 26 S proteasome. Mutant Rpt3 was assembled into intact PA700. This result indicates that intact PA700 can be assembled independently of association with 20 S proteasome and thus may be a direct precursor for 26 S proteasome assembly under normal conditions. These results provide new insights to the non-equivalent roles of Rpt subunits in 26 S proteasome function and identify specific roles for Rpt3.

Indexed as

Adenosine TriphosphatasesAmino Acid MotifsATPases Associated with Diverse Cellular ActivitiesBinding SitesCell LineCross-Linking ReagentsGlycerolHEK293 CellsHumansMutationProteasome Endopeptidase ComplexProtein Structure, TertiaryUbiquitinAdenosine TriphosphatasesATPases Associated with Diverse Cellular ActivitiesATP dependent 26S proteaseCross-Linking ReagentsGlycerolPA700 proteasome activatorProteasome Endopeptidase ComplexPSMC4 protein, humanUbiquitin

Identifiers

PMID20937828
PMCPMC2998155
OpenAlexW1982143936

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.