Evidence map›Paper›PMID 21784850›Full record

ArticleThe Journal of biological chemistry2011

Promotion of heat shock factor Hsf1 degradation via adaptor protein filamin A-interacting protein 1-like (FILIP-1L).

Yanzhong Hu, Nahid F Mivechi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
0.7field-weighted citation impact, top 31% 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

20 citing papers in PubMed, 33 citations in OpenAlex.

  1. Article
  2. Article
  3. 1-L Transcription of SARS-CoV-2 Spike Protein S1 Subunit.International journal of molecular sciences · 2024
    Article
  4. HSF1 and Its Role in Huntington's Disease Pathology.Advances in experimental medicine and biology · 2023
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. The heat-shock, or HSF1-mediated proteotoxic stress, response in cancer: from proteomic stability to oncogenesis.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. 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

2 authors at 2 institutions in 1 country.

Yanzhong HuCenter for Molecular Chaperone/Radiobiology and Cancer Virology, Georgia Health Sciences University, Augusta, Georgia 30912, USA.
Nahid F Mivechi
Augusta University Health · USCharlie Norwood VA Medical Center · US

Funding

Role of heat shock transcription factor HSF1 in tumoroginesisR01CA062130 · NCI · MEDICAL COLLEGE OF GEORGIA (MCG) · PI MIVECHI, NAHID F, MOSKOFIDIS, DIMITRIOS · 1996 to 2025
$9.0M
Role of heat shock factors (Hsfs) in tumorigenesisR01CA132640 · NCI · AUGUSTA UNIVERSITY · PI MIVECHI, NAHID F · 2008 to 2018
$2.7M
NCI NIH HHS CA062130NCI NIH HHS CA132640NCI NIH HHS R01 CA062130NCI NIH HHS R01 CA132640
6 · The paper itself

Abstract

Heat shock factor Hsf1 is involved in the regulation of a variety of cellular processes including heat shock response, development and differentiation, aging, and tumorigenesis. Hsf1 transcriptional activity is tightly controlled through phosphorylation, sumoylation, and acetylation, and through association with a number of regulatory proteins. However, regulation of Hsf1 protein stability or turnover remains unknown. We have identified a novel Hsf1-interacting protein, FILIP-1L, that was found to bind to Hsf1 through yeast two-hybrid screening. FILIP-1L encodes multiple isoforms spanning from 711 to 1135 amino acid residues. FILIP-1L contains four coiled-coil and two N-terminal leucine zipper domains. Ectopic expression of FILIP-1L reduces the expression of the Hsf1 protein because FILIP-1L promotes Hsf1 ubiquitination and degradation through the ubiquitin-proteasome system, leading to a reduction in Hsf1-mediated transcription. FILIP-1L, Hsf1, and the ubiquitin-binding domain of HhR23A, a receptor that transports polyubiquitinated proteins to the 19 S proteasome subunit targeting them for degradation, are found in a complex. This indicates that FILIP-1L is a potential adaptor that is involved in the Hsf1 degradation pathway. Taken together, our results indicate that FILIP-1L interacts with Hsf1, controlling its stability and thus modulating the heat shock response. These data indicate a novel function for FILIP-1L and a pathway for Hsf1 degradation through the ubiquitin-proteasome system.

Indexed as

AnimalsCarrier ProteinsCell LineCell Line, TumorContractile ProteinsCytoskeletal ProteinsDNA-Binding ProteinsFilaminsHeat-Shock ResponseHeat Shock Transcription FactorsHumansMiceMicrofilament ProteinsProteasome Endopeptidase ComplexProtein BindingTranscription FactorsCarrier ProteinsContractile ProteinsCytoskeletal ProteinsDNA-Binding ProteinsFilaminsFILIP1 protein, humanHeat Shock Transcription FactorsHSF1 protein, humanMicrofilament ProteinsProteasome Endopeptidase ComplexTranscription FactorsUbiquitin

Identifiers

PMID21784850
PMCPMC3173115
OpenAlexW2087115521

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.