Evidence map›Paper›PMID 17868456›Full record

ArticleBMC molecular biology2007

HAP1 can sequester a subset of TBP in cytoplasmic inclusions via specific interaction with the conserved TBP(CORE).

Justin R Prigge, Edward E Schmidt

Open access · hybridAbstract read
In one paragraph

Article in BMC molecular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.2field-weighted citation impact, top 51% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
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  5. Review
  6. Biological functions and potential therapeutic applications of huntingtin-associated protein 1: progress and prospects.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2022
    Review
  7. Article
  8. Article
  9. Article
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  11. DYRK1A regulates Hap1-Dcaf7/WDR68 binding with implication for delayed growth in Down syndrome.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  12. Article
  13. Article
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  15. Article
  16. 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

2 authors at 1 institution in 1 country.

Justin R PriggeVeterinary Molecular Biology, Molecular Biosciences, Montana State University, 960 Technology Blvd, Bozeman, MT 59717, USA. prigge@montana.edu
Edward E Schmidt
Montana State University · US

Funding

The Maternal/Fetal InteractionR01AI055739 · NIAID · MONTANA STATE UNIVERSITY - BOZEMAN · PI SCHMIDT, EDWARD E · 2005 to 2009
$1.7M
NIAID NIH HHS R01 AI055739NIAID NIH HHS R01 AI55739-01
6 · The paper itself

Abstract

backgroundHuntington's disease, spinal and bulbar muscular atrophy, and spinocerebellar ataxia 17 (SCA17) are caused by expansions in the polyglutamine (polyQ) repeats in Huntingtin protein (Htt), androgen receptor protein (AR), and TATA-binding protein (TBP), respectively. Htt-associated protein 1 (HAP1), a component of neuronal cytoplasmic stigmoid bodies (STBs), can sequester polyQ-expanded Htt and AR in STBs, thereby antagonizing formation of the nuclear aggregates associated with apoptotic neuron loss and disease progression.

resultsClones of HAP1 were isolated from unbiased two-hybrid screens for proteins that interact with TBP. Domain mapping showed that regions between amino acids 157 and 261 and between amino acids 473 and 582 of mouse HAP1 both bind specifically to the conserved C-terminal TBP(CORE) domain, away from the TBP N-terminal polyQ region. When fluorescently tagged versions of HAP1 or TBP were expressed independently in COS-7, 293, or Neuro-2a cells, all TBP localized to the nucleus and all HAP1 assembled into cytoplasmic stigmoid-like bodies (STLBs). When co-expressed, a portion of the TBP was assembled into the HAP1 STLBs while the remainder was localized to the nucleus. Although the TBP N terminus, including the polyQ region, was unnecessary for TBP-HAP1 interaction, in mammalian cells, removal of the TBP Q(repeat) reduced the proportion of TBP that assembled into STLBs, whereas expansion of the Q(repeat) had no significant affect on TBP subcellular localization.

conclusionHAP1 can sequester a subset of TBP protein away from the nucleus; extranuclear TBP sequestration is quantitatively influenced by the TBP polyQ repeat. These results suggest HAP1 could provide protection from SCA17 neuropathology.

Indexed as

AnimalsApoptosisCell LineCell NucleusCytoplasmGreen Fluorescent ProteinsHumansHuntingtin ProteinHuntington DiseaseImmunoprecipitationInclusion BodiesMiceNerve Tissue ProteinsNuclear ProteinsPeptidesProtein BindingGreen Fluorescent ProteinsHap1 protein, mouseHtt protein, mouseHuntingtin ProteinNerve Tissue ProteinsNuclear ProteinsPeptidespolyglutamineReceptors, AndrogenRecombinant Fusion ProteinsTATA-Box Binding Protein

Identifiers

PMID17868456
PMCPMC2082042
OpenAlexW2123970440

What OpenQuestion holds

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LicenceCC BY
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.