Evidence map›Paper›PMID 9236215›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience1997

Identification of a somatodendritic targeting signal in the cytoplasmic domain of the transferrin receptor.

A E West, R L Neve, K M Buckley

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing 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

38 citing papers in PubMed, 90 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Spatial control of membrane traffic in neuronal dendrites.Molecular and cellular neurosciences · 2020
    Review
  5. Recent Findings on AMPA Receptor Recycling.Frontiers in cellular neuroscience · 2018
    Review
  6. Article
  7. Ablation of TFR1 in Purkinje Cells Inhibits mGlu1 Trafficking and Impairs Motor Coordination, But Not Autistic-Like Behaviors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    Article
  8. Review
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Endocytosis of the glutamate receptor subunit GluK3 controls polarized trafficking.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011
    Article
  19. The role of iron in learning and memory.Advances in nutrition (Bethesda, Md.) · 2011
    Review
  20. The Sushi domains of GABAB receptors function as axonal targeting signals.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010
    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

3 authors at 2 institutions in 1 country.

A E WestDepartment of Neurobiology, Harvard Medical School, Boston, Massachusetts 02115, USA.
R L Neve
K M Buckley
Harvard University · USMcLean Hospital · US

Funding

EXPRESSION OF SYNAPTIC VESICLE PROTEINSR01NS027536 · NINDS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BUCKLEY, KATHLEEN M · 1991 to 1999
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DEVELOPMENTAL NEUROLOGYT32NS007009 · NINDS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BUCKLEY, KATHLEEN M · 1985 to 1999
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NINDS NIH HHS 2 T32 NS07009-21NINDS NIH HHS NS27536NINDS NIH HHS T32 NS007009
6 · The paper itself

Abstract

Neurons are highly polarized cells that must sort proteins synthesized in the cell body for transport into the axon or the dendrites. Given the amount of time and energy needed to deliver proteins to the distal processes, neurons must have high fidelity mechanisms that ensure proper polarized protein trafficking. Although a variety of proteins are localized either to the somatodendritic domain or to the axon (), the question of whether there are signal-dependent mechanisms that sort proteins to distinct neuronal domains is only beginning to be addressed. To determine sequence requirements for the polarized sorting of transmembrane proteins into dendrites, we expressed mutant transferrin receptors in cultured rat hippocampal neurons, using a defective herpes virus vector. Wild-type human transferrin receptor colocalized with the endogenous protein in dendritic endosomes and was strictly excluded from axons, despite overexpression. Polarized targeting was abolished by deletion of cytoplasmic amino acids 7-10, 11-14, or 19-28, but not 29-42 or 43-58. These deletions also increased the appearance of transferrin receptor on the plasma membrane, implying that endocytosis and dendritic targeting are mediated by overlapping signals and similar molecular mechanisms. In addition, we have characterized a specialized para-Golgi endosome poised to play a critical role in the polarized recycling of transmembrane proteins.

Indexed as

AnimalsCell PolarityCells, CulturedCytoplasmDendritesEndocytosisEndosomesFluorescent Antibody TechniqueHippocampusHumansMutagenesisNeuronsProtein Structure, TertiaryRatsRats, Sprague-DawleyReceptors, TransferrinReceptors, Transferrin

Identifiers

PMID9236215
PMCPMC6568350
OpenAlexW2107517282

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.