Evidence map›Paper›PMID 17978095›Full record

ArticleMolecular biology of the cell2008

Dynamic association of the fragile X mental retardation protein as a messenger ribonucleoprotein between microtubules and polyribosomes.

Houping Wang, Jason B Dictenberg, Li Ku, Wen Li, Gary J Bassell, Yue Feng

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
4.3field-weighted citation impact, top 5% 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

31 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. FMRP and Ataxin-2 function together in long-term olfactory habituation and neuronal translational control.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  15. Review
  16. Reactivation of stalled polyribosomes in synaptic plasticity.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  17. New perspectives on the biology of fragile X syndrome.Current opinion in genetics & development · 2012
    Review
  18. Article
  19. Interaction of survival of motor neuron (SMN) and HuD proteins with mRNA cpg15 rescues motor neuron axonal deficits.Proceedings of the National Academy of Sciences of the United States of America · 2011
    Article
  20. 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.

Houping WangDepartment of Pharmacology, Emory University School of Medicine, Atlanta, GA 30322, USA.
Jason B Dictenberg
Li Ku
Wen Li
Gary J Bassell
Yue Feng
Emory University · USAlbert Einstein College of Medicine · US

Funding

TRANSCRIPTION AND RNA BINDING IN FRAGILE X SYNDROMEP01HD035576 · NICHD · EMORY UNIVERSITY · PI WARREN, STEPHEN T. · 1997 to 2005
$5.0M
Imaging FMRP Regulation and FunctionR01NS051127 · NINDS · EMORY UNIVERSITY · PI BASSELL, GARY J · 2005 to 2008
$1.3M
NICHD NIH HHS 5P01 HD-35576NICHD NIH HHS P01 HD035576NINDS NIH HHS NS-051127NINDS NIH HHS R01 NS051127
6 · The paper itself

Abstract

The fragile X mental retardation protein (FMRP) is a selective RNA-binding protein that regulates translation and plays essential roles in synaptic function. FMRP is bound to specific mRNA ligands, actively transported into neuronal processes in a microtubule-dependent manner, and associated with polyribosomes engaged in translation elongation. However, the biochemical relationship between FMRP-microtubule association and FMRP-polyribosome association remains elusive. Here, we report that although the majority of FMRP is incorporated into elongating polyribosomes in the soluble cytoplasm, microtubule-associated FMRP is predominantly retained in translationally dormant, polyribosome-free messenger ribonucleoprotein (mRNP) complexes. Interestingly, FMRP-microtubule association is increased when mRNPs are dynamically released from polyribosomes as a result of inhibiting translation initiation. Furthermore, the I304N mutant FMRP that fails to be incorporated into polyribosomes is associated with microtubules in mRNP particles and transported into neuronal dendrites in a microtubule-dependent, 3,5-dihydroxyphenylglycine-stimulated manner with similar kinetics to that of wild-type FMRP. Hence, polyribosome-free FMRP-mRNP complexes travel on microtubules and wait for activity-dependent translational derepression at the site of function. The dual participation of FMRP in dormant mRNPs and polyribosomes suggests distinct roles of FMRP in dendritic transport and translational regulation, two distinct phases that control local protein production to accommodate synaptic plasticity.

Indexed as

ActinsAnimalsAsparagineCell LineDendritesFragile X Messenger Ribonucleoprotein 1HumansIsoleucineKineticsMethoxyhydroxyphenylglycolMiceMicrotubulesMutant ProteinsMutationPolyribosomesProtein Transport3,4-dihydroxyphenylglycolActinsAsparagineFragile X Messenger Ribonucleoprotein 1Isoleucinemessenger ribonucleoproteinMethoxyhydroxyphenylglycolMutant ProteinsReceptors, Metabotropic GlutamateRibonucleasesRibonucleoproteins

Identifiers

PMID17978095
PMCPMC2174202
OpenAlexW2107314617

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.