Evidence map›Paper›PMID 17347650›Full record

ArticleThe EMBO journal2007

Post-phosphorylation prolyl isomerisation of gephyrin represents a mechanism to modulate glycine receptors function.

M Moretto Zita, Ivan Marchionni, Elisa Bottos, Massimo Righi, Giannino Del Sal, Enrico Cherubini, Paola Zacchi

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
2.8field-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

55 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Article
  3. Pin1 promotes human CaCell communication and signaling : CCS · 2024
    Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
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  10. Review
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  13. TheMedical research archives · 2020
    Article
  14. Review
  15. Review
  16. Article
  17. Structure-Function Relationships of Glycine and GABAFrontiers in molecular neuroscience · 2018
    Review
  18. Article
  19. 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

7 authors at 2 institutions in 1 country.

M Moretto ZitaInternational School for Advanced Studies, Neuroscience Programme, Area Science Park, Basovissa SS14, 34012 Trieste, Italy.
Ivan Marchionni
Elisa Bottos
Massimo Righi
Giannino Del Sal
Enrico Cherubini
Paola Zacchi
Scuola Internazionale Superiore di Studi Avanzati · ITAREA Science Park · IT

Funding

BIOLOGICAL ROLES OF THE PROLYL ISOMERASE, PIN1R01CA082845 · NCI · DUKE UNIVERSITY · PI MEANS, ANTHONY R · 1999 to 2009
$2.9M
NCI NIH HHS CA 082845NCI NIH HHS R01 CA082845
6 · The paper itself

Abstract

The microtubule binding protein gephyrin plays a prominent role in establishing and maintaining a high concentration of inhibitory glycine receptors juxtaposed to presynaptic releasing sites. Here, we show that endogenous gephyrin undergoes proline-directed phosphorylation, which is followed by the recruitment of the peptidyl-prolyl isomerase Pin1. The interaction between gephyrin and Pin1 is strictly dependent on gephyrin phosphorylation and requires serine-proline consensus sites encompassing the gephyrin proline-rich domain. Upon binding, Pin1 triggers conformational changes in the gephyrin molecule, thus enhancing its ability to bind the beta subunit of GlyRs. Consistently, a downregulation of GlyR clusters was detected in hippocampal neurons derived from Pin1 knockout mice, which was paralleled by a reduction in the amplitude of glycine-evoked currents. Our results suggest that phosphorylation-dependent prolyl isomerisation of gephyrin represents a mechanism for regulating GlyRs function.

Indexed as

AnimalsBrainCarrier ProteinsCytoplasmic StructuresEpitopesEvoked PotentialsHippocampusHumansMembrane ProteinsMiceMice, KnockoutNeuronsNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePhosphorylationProlineCarrier ProteinsEpitopesgephyrinMembrane ProteinsNIMA-Interacting Peptidylprolyl IsomerasePeptidylprolyl IsomerasePIN1 protein, humanPin1 protein, mouseProlineProtein SubunitsReceptors, GlycineRecombinant ProteinsSerine

Identifiers

PMID17347650
PMCPMC1847658
OpenAlexW2086783898

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.