Evidence map›Paper›PMID 22955284›Full record

ArticleThe Journal of biological chemistry2012

Nectin-1 binds and signals through the fibroblast growth factor receptor.

Kirsten B Bojesen, Ole Clausen, Kristian Rohde, Claus Christensen, Lanjun Zhang, Shizhong Li, Lene Køhler, Steen Nielbo, Janne Nielsen, Michelle D Gjørlund and 3 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed, 1 pooled it
1.2field-weighted citation impact, top 25% 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, 1 synthesis or guideline pooled it, 36 citations in OpenAlex.

  1. Cell adhesion and intracellular calcium signaling in neurons.Cell communication and signaling : CCS · 2013
    Pooled it
  2. Article
  3. Article
  4. Nectin-2 in general and in the brain.Molecular and cellular biochemistry · 2022
    Review
  5. Article
  6. Review
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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

13 authors at 1 institution in 1 country.

Kirsten B BojesenProtein Laboratory, Department of Neuroscience and Pharmacology, Panum Institute, Blegdamsvej 3C, DK-2200 Copenhagen, Denmark.
Ole Clausen
Kristian Rohde
Claus Christensen
Lanjun Zhang
Shizhong Li
Lene Køhler
Steen Nielbo
Janne Nielsen
Michelle D Gjørlund
Flemming M Poulsen
Elisabeth Bock
Vladimir Berezin
University of Copenhagen · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Nectins belong to a family of immunoglobulin (Ig)-like cell-adhesion molecules comprising four members, nectin-1 through nectin-4. Nectins are involved in formation of the mechanical adhesive puncta adherentia junctions of synapses. Nectins share the same overall structural topology with an extracellular region containing three Ig modules, a transmembrane region, and a cytoplasmic region. In nectin-1, the first and second Ig module in the extracellular region are necessary for the trans-interaction with nectin-3 and formation of cis-dimers, respectively. The function of the third Ig module of nectin-1 remains unknown. We here report the structure in solution of the third, membrane-proximal Ig module of mouse nectin-1 (nectin-1 Ig3) solved by means of nuclear magnetic resonance (NMR) spectroscopy. It belongs to the C1 set of the Ig superfamily. Nectin-1 Ig3 was produced as a recombinant protein and induced neurite outgrowth in primary cultures of hippocampal and cerebellar granule neurons, an effect abolished by treatment with the fibroblast growth factor receptor (FGFR) inhibitor SU5402, or by transfection with a dominant-negative FGFR1 construct. We showed by surface plasmon resonance (SPR) analysis that nectin-1 Ig3 directly interacted with various isoforms of FGFR. Nectin-1 Ig3 induced phosphorylation of FGFR1c in the same manner as the whole nectin-1 ectodomain, and promoted survival of cerebellar granule neurons induced to undergo apoptosis. Finally, we constructed a peptide, nectide, by employing in silico modeling of various FGFR ligand-binding sites. Nectide mimicked all the effects of nectin-1 Ig3. We suggest that FGFR is a downstream signaling partner of nectin-1.

Indexed as

Amino Acid SequenceAnimalsApoptosisCell Adhesion MoleculesCell SurvivalCrystallography, X-RayFibroblast Growth Factor 2HEK293 CellsHippocampusHumansMiceMolecular Sequence DataNectinsNeuritesNeuronsPhosphorylationCell Adhesion MoleculesFGFR1 protein, humanFibroblast Growth Factor 2NECTIN1 protein, humanNectin1 protein, mouseNECTIN3 protein, humanNectin3 protein, mouseNectinsProtein IsoformsReceptor, Fibroblast Growth Factor, Type 1Receptors, Platelet-Derived Growth Factor

Identifiers

PMID22955284
PMCPMC3481338
OpenAlexW2056151358

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.