Evidence map›Paper›PMID 32737405›Full record

ArticleCommunications biology2020

Control of protein palmitoylation by regulating substrate recruitment to a zDHHC-protein acyltransferase.

Fiona Plain, Jacqueline Howie, Jennifer Kennedy, Elaine Brown, Michael J Shattock, Niall J Fraser, William Fuller

Open access · goldAbstract read
In one paragraph

Article in Communications biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.6field-weighted citation impact, top 4% 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

40 citing papers in PubMed, 78 citations in OpenAlex.

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  13. Mechanisms and functions of protein S-acylation.Nature reviews. Molecular cell biology · 2024
    Review
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  20. Journal of proteome research · 2023
    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 3 institutions in 1 country.

Fiona Plain *School of Medicine, University of Dundee, Dundee, UK.
Jacqueline Howie *Institute of Cardiovascular and Medical Sciences, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, UK.
Jennifer KennedyInstitute of Cardiovascular and Medical Sciences, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, UK.
Elaine BrownInstitute of Cardiovascular and Medical Sciences, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, UK.
Michael J ShattockCardiovascular Division, The Rayne Institute, King's College London, London, UK.ORCID http://orcid.org/0000-0001-6242-7585
Niall J FraserSchool of Medicine, University of Dundee, Dundee, UK. n.fraser@dundee.ac.uk.ORCID http://orcid.org/0000-0001-7349-5647
William FullerInstitute of Cardiovascular and Medical Sciences, College of Medical, Veterinary and Life Sciences, University of Glasgow, Glasgow, UK. will.fuller@glasgow.ac.uk.ORCID http://orcid.org/0000-0002-5883-4433
University of Glasgow · GBUniversity of Dundee · GBKing's College London · GB

Funding

British Heart Foundation FS/14/68/30988British Heart Foundation PG/16/33/32134British Heart Foundation PG/18/60/33957British Heart Foundation PG/19/5/34150British Heart Foundation RG/17/15/33106British Heart Foundation SP/16/3/32317Medical Research Council G0700903
6 · The paper itself

Abstract

Although palmitoylation regulates numerous cellular processes, as yet efforts to manipulate this post-translational modification for therapeutic gain have proved unsuccessful. The Na-pump accessory sub-unit phospholemman (PLM) is palmitoylated by zDHHC5. Here, we show that PLM palmitoylation is facilitated by recruitment of the Na-pump α sub-unit to a specific site on zDHHC5 that contains a juxtamembrane amphipathic helix. Site-specific palmitoylation and GlcNAcylation of this helix increased binding between the Na-pump and zDHHC5, promoting PLM palmitoylation. In contrast, disruption of the zDHHC5-Na-pump interaction with a cell penetrating peptide reduced PLM palmitoylation. Our results suggest that by manipulating the recruitment of specific substrates to particular zDHHC-palmitoyl acyl transferases, the palmitoylation status of individual proteins can be selectively altered, thus opening the door to the development of molecular modulators of protein palmitoylation for the treatment of disease.

Indexed as

AcetyltransferasesAcyltransferasesAnimalsCell MembraneCell-Penetrating PeptidesHumansLipoylationMembrane ProteinsMicePhosphoproteinsPhosphorylationProtein Processing, Post-TranslationalRatsSodium-Potassium-Exchanging ATPaseSubstrate SpecificityAcetyltransferasesAcyltransferasesCell-Penetrating PeptidesMembrane ProteinsphospholemmanPhosphoproteinsprotein acyltransferaseSodium-Potassium-Exchanging ATPaseZDHHC5 protein, human

Identifiers

PMID32737405
PMCPMC7395175
OpenAlexW3046881056

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.