Evidence map›Paper›PMID 22844492›Full record

ArticlePloS one2012

Protein tyrosine phosphatase PTP1B is involved in hippocampal synapse formation and learning.

Federico Fuentes, Derek Zimmer, Marybless Atienza, Jamie Schottenfeld, Ian Penkala, Tracy Bale, Kendra K Bence, Carlos O Arregui

Abstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
–field-weighted citation impact
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

28 citing papers in PubMed.

  1. The tyrosine phosphatase STEP is a developmental suppressor of synaptogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Article
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  4. Article
  5. Alpha-Linolenic Acid Ameliorates Cognitive Impairment and Liver Damage Caused by Obesity.Diabetes, metabolic syndrome and obesity : targets and therapy · 2024
    Article
  6. Article
  7. Review
  8. Article
  9. Allosteric Inhibition of PTP1B by a Nonpolar Terpenoid.The journal of physical chemistry. B · 2022
    Article
  10. Article
  11. Peroxisomal Proliferator-Activated ReceptorFrontiers in pharmacology · 2022
    Article
  12. Role of Aβ in Alzheimer's-related synaptic dysfunction.Frontiers in cell and developmental biology · 2022
    Review
  13. Article
  14. Article
  15. Exploring the Therapeutic Potential of Protein Tyrosine Phosphatase 1B in hAPP-J20 Mouse Model of Alzheimer's Disease.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  16. Article
  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

8 authors.

Federico FuentesInstituto de Investigaciones Biotecnológicas, Universidad de San Martín/CONICET, San Martín, Buenos Aires, Argentina.
Derek Zimmer
Marybless Atienza
Jamie Schottenfeld
Ian Penkala
Tracy Bale
Kendra K Bence
Carlos O Arregui

Funding

Neuronal Protein Tyrosine Phosphatases in MetabolismR01DK082417 · NIDDK · UNIVERSITY OF PENNSYLVANIA · PI BENCE, KENDRA · 2009 to 2015
$2.6M
NIDDK NIH HHS DK082417NIDDK NIH HHS R01 DK082417
6 · The paper itself

Abstract

ER-bound PTP1B is expressed in hippocampal neurons, and accumulates among neurite contacts. PTP1B dephosphorylates ß-catenin in N-cadherin complexes ensuring cell-cell adhesion. Here we show that endogenous PTP1B, as well as expressed GFP-PTP1B, are present in dendritic spines of hippocampal neurons in culture. GFP-PTP1B overexpression does not affect filopodial density or length. In contrast, impairment of PTP1B function or genetic PTP1B-deficiency leads to increased filopodia-like dendritic spines and a reduction in mushroom-like spines, while spine density is unaffected. These morphological alterations are accompanied by a disorganization of pre- and post-synapses, as judged by decreased clustering of synapsin-1 and PSD-95, and suggest a dynamic synaptic phenotype. Notably, levels of ß-catenin-Tyr-654 phosphorylation increased ∼5-fold in the hippocampus of adult PTP1B(-/-) (KO) mice compared to wild type (WT) mice and this was accompanied by a reduction in the amount of ß-catenin associated with N-cadherin. To determine whether PTP1B-deficiency alters learning and memory, we generated mice lacking PTP1B in the hippocampus and cortex (PTP1B(fl/fl)-Emx1-Cre). PTP1B(fl/fl)-Emx1-Cre mice displayed improved performance in the Barnes maze (decreased time to find and enter target hole), utilized a more efficient strategy (cued), and had better recall compared to WT controls. Our results implicate PTP1B in structural plasticity within the hippocampus, likely through modulation of N-cadherin function by ensuring dephosphorylation of ß-catenin on Tyr-654. Disruption of hippocampal PTP1B function or expression leads to elongation of dendritic filopodia and improved learning and memory, demonstrating an exciting novel role for this phosphatase.

Indexed as

LearningAnimalsbeta CateninCadherinsDendritic SpinesFemaleGene DeletionHippocampusMemoryMiceNeuronal PlasticityPhosphorylationPregnancyProtein TransportProtein Tyrosine Phosphatase, Non-Receptor Type 1Ratsbeta CateninCadherinsProtein Tyrosine Phosphatase, Non-Receptor Type 1Ptpn1 protein, mousePtpn1 protein, ratTyrosine

Identifiers

PMID22844492
PMCPMC3402386

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Read underepoch 390

Registered trials

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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.