Evidence map›Paper›PMID 26334723›Full record

ArticleNature communications2015

Activity-regulated trafficking of the palmitoyl-acyl transferase DHHC5.

G Stefano Brigidi, Brendan Santyr, Jordan Shimell, Blair Jovellar, Shernaz X Bamji

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 72 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
72citing papers in PubMed, 1 pooled it
3.8field-weighted citation impact, top 6% 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

72 citing papers in PubMed, 1 synthesis or guideline pooled it, 120 citations in OpenAlex.

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  18. Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024
    Review
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12 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

G Stefano BrigidiDepartment of Cellular and Physiological Sciences, and the Djavad Mowafaghian Center for Brain Health, University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia, Canada, V6T-1Z3.
Brendan SantyrDepartment of Cellular and Physiological Sciences, and the Djavad Mowafaghian Center for Brain Health, University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia, Canada, V6T-1Z3.
Jordan ShimellDepartment of Cellular and Physiological Sciences, and the Djavad Mowafaghian Center for Brain Health, University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia, Canada, V6T-1Z3.
Blair JovellarDepartment of Cellular and Physiological Sciences, and the Djavad Mowafaghian Center for Brain Health, University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia, Canada, V6T-1Z3.
Shernaz X BamjiDepartment of Cellular and Physiological Sciences, and the Djavad Mowafaghian Center for Brain Health, University of British Columbia, 2350 Health Sciences Mall, Vancouver, British Columbia, Canada, V6T-1Z3.
University of British Columbia · CA

Funding

Canadian Institutes of Health Research MOP-81144Canadian Institutes of Health Research MOP-81158
6 · The paper itself

Abstract

Synaptic plasticity is mediated by the dynamic localization of proteins to and from synapses. This is controlled, in part, through activity-induced palmitoylation of synaptic proteins. Here we report that the ability of the palmitoyl-acyl transferase, DHHC5, to palmitoylate substrates in an activity-dependent manner is dependent on changes in its subcellular localization. Under basal conditions, DHHC5 is bound to PSD-95 and Fyn kinase, and is stabilized at the synaptic membrane through Fyn-mediated phosphorylation of a tyrosine residue within the endocytic motif of DHHC5. In contrast, DHHC5's substrate, δ-catenin, is highly localized to dendritic shafts, resulting in the segregation of the enzyme/substrate pair. Neuronal activity disrupts DHHC5/PSD-95/Fyn kinase complexes, enhancing DHHC5 endocytosis, its translocation to dendritic shafts and its association with δ-catenin. Following DHHC5-mediated palmitoylation of δ-catenin, DHHC5 and δ-catenin are trafficked together back into spines where δ-catenin increases cadherin stabilization and recruitment of AMPA receptors to the synaptic membrane.

Indexed as

AcyltransferasesAnimalsBlotting, WesternCateninsDelta CateninDendritesDisks Large Homolog 4 ProteinEndocytosisHEK293 CellsHippocampusHumansImage Processing, Computer-AssistedImmunohistochemistryImmunoprecipitationIntracellular Signaling Peptides and ProteinsLipoylationAcyltransferasesCateninsDelta CateninDisks Large Homolog 4 ProteinDlg4 protein, ratIntracellular Signaling Peptides and ProteinsMembrane ProteinsProto-Oncogene Proteins c-fynZdhhc5 protein, rat

Identifiers

PMID26334723
PMCPMC4569850
OpenAlexW1260662944

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.