Evidence map›Paper›PMID 26608278›Full record

ArticleBMC cell biology2015

The clustered protocadherin endolysosomal trafficking motif mediates cytoplasmic association.

Adam Shonubi, Chantelle Roman, Greg R Phillips

Abstract read
In one paragraph

Article in BMC cell biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Surface delivery quantification reveals distinct trafficking efficiencies among clustered protocadherin isoforms.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Article
  4. Article
  5. A Unique Role for Protocadherin γC3 in Promoting Dendrite Arborization through an Axin1-Dependent Mechanism.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
    Article
  6. Article
  7. Article
  8. Article
  9. The γ-Protocadherins Regulate the Survival of GABAergic Interneurons during Developmental Cell Death.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  10. Expression of protocadherin-γC4 protein in the rat brain.The Journal of comparative neurology · 2020
    Article
  11. Review
  12. Protocadherins at the Crossroad of Signaling Pathways.Frontiers in molecular neuroscience · 2020
    Review
  13. 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.

Adam ShonubiDepartment of Biology, College of Staten Island, City University of New York, 2800 Victory Blvd, Staten Island, NY, 10314, USA. adam.shonubi@cix.csi.cuny.edu.
Chantelle RomanDepartment of Biology, College of Staten Island, City University of New York, 2800 Victory Blvd, Staten Island, NY, 10314, USA. chantelle.roman@cix.csi.cuny.edu.
Greg R PhillipsDepartment of Biology, College of Staten Island, City University of New York, 2800 Victory Blvd, Staten Island, NY, 10314, USA. greg.phillips@csi.cuny.edu.

Funding

Recognition coding at CNS synapsesR01NS051238 · NINDS · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI PHILLIPS, GREG R · 2006 to 2010
$1.7M
NINDS NIH HHS R01 NS051238NINDS NIH HHS R01NS051238
6 · The paper itself

Abstract

backgroundClustered protocadherins (Pcdhs) are a large family of neural cadherin-like proteins encoded by individual exons located within three gene clusters. Each exon codes an extracellular, transmembrane, and proximal cytoplasmic domain. These "variable" regions may be spliced to a constant cytoplasmic moiety encoded at the end of a cluster. Pcdh extracellular domains mediate homophilic cell-cell binding but their cytoplasmic domains cause intracellular retention and may negatively regulate Pcdh cell-cell binding. Pcdhs can be found at the cell surface in neurons and other cells but are also, unlike classical cadherins, prominently trafficked to the endolysosome system. It was previously found that a segment within the variable portion of the Pcdh-γA3 cytoplasmic domain (VCD) was shown to be necessary for endolysosomal trafficking.

resultsHere it is shown that this same VCD segment can mediate cytoplasmic association among Pcdhs from the different clusters. Internal deletions within this VCD region (termed here the VCD motif) that disrupt the association altered trafficking of Pcdh-γA3 in the endolysosomal system while deletions outside VCD motif did not affect trafficking.

conclusionsThe results show that Pcdhs associate cytoplasmically via a motif within the VCD and that this is critical for Pcdh trafficking. Given that truncation at the VCD motif alters endolysosomal trafficking of Pcdhs, the VCD interaction described here may provide new insights into the dynamic nature of Pcdh mediated cell-cell interactions.

Indexed as

Amino Acid MotifsCadherin Related ProteinsCadherinsCytoplasmEndosomesHumansLysosomesMolecular Sequence DataProtein TransportCadherin Related ProteinsCadherinsPCDH-GAMMA-A3, human

Identifiers

PMID26608278
PMCPMC4660814

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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.