Evidence map›Paper›PMID 18573886›Full record

ArticleMolecular and cellular biology2008

Chaperone Hsp27, a novel subunit of AUF1 protein complexes, functions in AU-rich element-mediated mRNA decay.

Kristina S Sinsimer, Frances M Gratacós, Anna M Knapinska, Jiebo Lu, Christopher D Krause, Alexandria V Wierzbowski, Lauren R Maher, Shannon Scrudato, Yonaira M Rivera, Swati Gupta and 4 more

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
2.6field-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

48 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
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  4. Article
  5. Relationship betweenJournal of thoracic disease · 2021
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  13. Non-alcoholic fatty liver disease phosphoproteomics: A functional piece of the precision puzzle.Hepatology research : the official journal of the Japan Society of Hepatology · 2017
    Article
  14. Article
  15. AUF1 regulation of coding and noncoding RNA.Wiley interdisciplinary reviews. RNA · 2017
    Review
  16. Review
  17. Article
  18. Article
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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

14 authors at 1 institution in 1 country.

Kristina S SinsimerDepartment of Molecular Genetics, Microbiology and Immunology, UMDNJ-Robert Wood Johnson Medical School, 675 Hoes Lane, Piscataway, NJ 08854, USA.
Frances M Gratacós
Anna M Knapinska
Jiebo Lu
Christopher D Krause
Alexandria V Wierzbowski
Lauren R Maher
Shannon Scrudato
Yonaira M Rivera
Swati Gupta
Danielle K Turrin
Mary Pauline De La Cruz
Sidney Pestka
Gary Brewer
Johnson University · US

Funding

Translational Regulation by the TNF Alpha AU-rich ElementP01AI057596 · NIAID · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI PESTKA, SIDNEY · 2004 to 2009
$8.8M
Inter-University Doctoral Degree:Puerto Rico to RutgersR25GM058389 · NIGMS · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI LANGER, JEROME ALAN, RIOS-VELAZQUEZ, CARLOS · 1998 to 2016
$3.0M
Receptor-Signaling Protein Interactions in Real TimeR01AI059465 · NIAID · UNIV OF MED/DENT NJ-R W JOHNSON MED SCH · PI PESTKA, SIDNEY · 2004 to 2007
$1.4M
PHASE 1 CLINICAL TRIAL OF IL 10 IN HIV INFECTED AND UNINFECTED INDIVIDUALSZ01AI000743 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI WEISSSMAN, D · 1996 to 1997
–
NIAID NIH HHS P01 AI057596NIAID NIH HHS R01 AI059465NIAID NIH HHS T32 AI00743NIGMS NIH HHS R25 GM058389
6 · The paper itself

Abstract

Controlled, transient cytokine production by monocytes depends heavily upon rapid mRNA degradation, conferred by 3' untranslated region-localized AU-rich elements (AREs) that associate with RNA-binding proteins. The ARE-binding protein AUF1 forms a complex with cap-dependent translation initiation factors and heat shock proteins to attract the mRNA degradation machinery. We refer to this protein assembly as the AUF1- and signal transduction-regulated complex, ASTRC. Rapid degradation of ARE-bearing mRNAs (ARE-mRNAs) requires ubiquitination of AUF1 and its destruction by proteasomes. Activation of monocytes by adhesion to capillary endothelium at sites of tissue damage and subsequent proinflammatory cytokine induction are prominent features of inflammation, and ARE-mRNA stabilization plays a critical role in the induction process. Here, we demonstrate activation-induced subunit rearrangements within ASTRC and identify chaperone Hsp27 as a novel subunit that is itself an ARE-binding protein essential for rapid ARE-mRNA degradation. As Hsp27 has well-characterized roles in protein ubiquitination as well as in adhesion-induced cytoskeletal remodeling and cell motility, its association with ASTRC may provide a sensing mechanism to couple proinflammatory cytokine induction with monocyte adhesion and motility.

Indexed as

RNA StabilityCell Line, TumorCell SurvivalFluorescence Resonance Energy TransferHeat-Shock ProteinsHeterogeneous-Nuclear Ribonucleoprotein DHeterogeneous Nuclear Ribonucleoprotein D0HSP27 Heat-Shock ProteinsHumansMolecular ChaperonesMultiprotein ComplexesNeoplasm ProteinsProtein BindingProtein SubunitsRegulatory Sequences, Ribonucleic AcidTumor Necrosis Factor-alphaHeat-Shock ProteinsHeterogeneous-Nuclear Ribonucleoprotein DHeterogeneous Nuclear Ribonucleoprotein D0HNRNPD protein, humanHSP27 Heat-Shock ProteinsHSPB1 protein, humanMolecular ChaperonesMultiprotein ComplexesNeoplasm ProteinsProtein SubunitsRegulatory Sequences, Ribonucleic AcidTumor Necrosis Factor-alpha

Identifiers

PMID18573886
PMCPMC2519747
OpenAlexW2156588282

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.