Evidence map›Paper›PMID 19398583›Full record

ArticleMolecular and cellular biology2009

The yeast AAA+ chaperone Hsp104 is part of a network that links the actin cytoskeleton with the inheritance of damaged proteins.

Peter Tessarz, Michael Schwarz, Axel Mogk, Bernd Bukau

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

45 citing papers in PubMed, 75 citations in OpenAlex.

  1. Article
  2. Article
  3. Quiescence inAnnual review of genetics · 2022
    Review
  4. Article
  5. Differential Interactions of Molecular Chaperones and Yeast Prions.Journal of fungi (Basel, Switzerland) · 2022
    Review
  6. Review
  7. Review
  8. Article
  9. Protein aggregation in bacteria.FEMS microbiology reviews · 2020
    Review
  10. Article
  11. Spiraling in Control: Structures and Mechanisms of the Hsp104 Disaggregase.Cold Spring Harbor perspectives in biology · 2019
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. The life of [PSI].Current genetics · 2018
    Review
  17. Review
  18. De novo [PSIScientific reports · 2017
    Article
  19. Review
  20. Prions, Chaperones, and Proteostasis in Yeast.Cold Spring Harbor perspectives in biology · 2017
    Review
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 3 institutions in 1 country.

Peter TessarzUniversität Heidelberg, Zentrum fuer Molekulare Biologie Heidelberg, DKFZ-ZMBH Alliance, Im Neuenheimer Feld 282, Heidelberg D-69120, Germany.
Michael Schwarz
Axel Mogk
Bernd Bukau
DKFZ-ZMBH Alliance · DEHeidelberg University · DEMax Planck Institute of Biochemistry · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The yeast AAA(+) chaperone Hsp104 is essential for the development of thermotolerance and for the inheritance of prions. Recently, Hsp104, together with the actin cytoskeleton, has been implicated in the asymmetric distribution of carbonylated proteins. Here, we investigated the interplay between Hsp104 and actin by using a dominant-negative variant of Hsp104 (HAP/ClpP) that degrades substrate proteins instead of remodeling them. Coexpression of HAP/ClpP causes defects in morphology and the actin cytoskeleton. Taking a candidate approach, we identified Spa2, a member of the polarisome complex, as an Hsp104 substrate. Furthermore, we provided genetic evidence that links Spa2 and Hsp104 to Hof1, a member of the cytokinesis machinery. Spa2 and Hof1 knockout cells are affected in the asymmetric distribution of damaged proteins, suggesting that Hsp104, Spa2, and Hof1 are members of a network controlling the inheritance of carbonylated proteins.

Indexed as

ActinsCytoskeletal ProteinsCytoskeletonHeat-Shock ProteinsMicrotubule-Associated ProteinsMolecular ChaperonesOxidation-ReductionProtein CarbonylationRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsActinsCytoskeletal ProteinsHeat-Shock ProteinsHOF1 protein, S cerevisiaeHsP104 protein, S cerevisiaeMicrotubule-Associated ProteinsMolecular ChaperonesRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSPA2 protein, S cerevisiae

Identifiers

PMID19398583
PMCPMC2698747
OpenAlexW2162179975

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.