Evidence map›Paper›PMID 17634286›Full record

ArticleMolecular biology of the cell2007

ADD66, a gene involved in the endoplasmic reticulum-associated degradation of alpha-1-antitrypsin-Z in yeast, facilitates proteasome activity and assembly.

Craig M Scott, Kristina B Kruse, Béla Z Schmidt, David H Perlmutter, Ardythe A McCracken, Jeffrey L Brodsky

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing 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

19 citing papers in PubMed, 33 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Assembly of the 20S proteasome.Biochimica et biophysica acta · 2014
    Review
  10. Review
  11. Article
  12. Review
  13. Proteostasis: a new therapeutic paradigm for pulmonary disease.Proceedings of the American Thoracic Society · 2011
    Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Molecular mechanisms of proteasome assembly.Nature reviews. Molecular cell biology · 2009
    Review
  19. 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

6 authors at 2 institutions in 1 country.

Craig M ScottDepartment of Biological Sciences, University of Pittsburgh, Pittsburgh, PA 15260, USA.
Kristina B Kruse
Béla Z Schmidt
David H Perlmutter
Ardythe A McCracken
Jeffrey L Brodsky
University of Pittsburgh · USUniversity of Nevada, Reno · US

Funding

ER Associated Degradation of Membrane Proteins in YeastR01GM075061 · NIGMS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI BRODSKY, JEFFREY L. · 2006 to 2019
$3.2M
LOCAL EXPRESSION OF ALPHA-1-ANTITRYPSIN IN EMPHYSEMAR01HL037784 · NHLBI · WASHINGTON UNIVERSITY · PI PERLMUTTER, DAVID H · 1986 to 2008
$3.0M
LIVER INJURY IN ALPHA 1 ANTITRYPSIN DEFICIENCYR01DK052526 · NIDDK · WASHINGTON UNIVERSITY · PI PERLMUTTER, DAVID H · 1997 to 2007
$2.2M
NHLBI NIH HHS HL-037784NHLBI NIH HHS R01 HL037784NIDDK NIH HHS DK-052526NIDDK NIH HHS R01 DK052526NIGMS NIH HHS GM-75061NIGMS NIH HHS R01 GM075061
6 · The paper itself

Abstract

Antitrypsin deficiency is a primary cause of juvenile liver disease, and it arises from expression of the "Z" variant of the alpha-1 protease inhibitor (A1Pi). Whereas A1Pi is secreted from the liver, A1PiZ is retrotranslocated from the endoplasmic reticulum (ER) and degraded by the proteasome, an event that may offset liver damage. To better define the mechanism of A1PiZ degradation, a yeast expression system was developed previously, and a gene, ADD66, was identified that facilitates A1PiZ turnover. We report here that ADD66 encodes an approximately 30-kDa soluble, cytosolic protein and that the chymotrypsin-like activity of the proteasome is reduced in add66Delta mutants. This reduction in activity may arise from the accumulation of 20S proteasome assembly intermediates or from qualitative differences in assembled proteasomes. Add66p also seems to be a proteasome substrate. Consistent with its role in ER-associated degradation (ERAD), synthetic interactions are observed between the genes encoding Add66p and Ire1p, a transducer of the unfolded protein response, and yeast deleted for both ADD66 and/or IRE1 accumulate polyubiquitinated proteins. These data identify Add66p as a proteasome assembly chaperone (PAC), and they provide the first link between PAC activity and ERAD.

Indexed as

Protein Processing, Post-Translationalalpha 1-AntitrypsinChymotrypsinCytosolEndoplasmic ReticulumGene DeletionGenes, FungalMembrane GlycoproteinsProteasome Endopeptidase ComplexProtein FoldingProtein PrecursorsProtein Serine-Threonine KinasesProtein SubunitsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSolubilityalpha 1-AntitrypsinChymotrypsinIRE1 protein, S cerevisiaeMembrane GlycoproteinsProteasome Endopeptidase ComplexProtein PrecursorsProtein Serine-Threonine KinasesProtein SubunitsSaccharomyces cerevisiae Proteins

Identifiers

PMID17634286
PMCPMC1995736
OpenAlexW2116559137

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.