Evidence map›Paper›PMID 25271157›Full record

ArticleThe Journal of biological chemistry2014

Identification of palmitoyltransferase and thioesterase enzymes that control the subcellular localization of axon survival factor nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2).

Stefan Milde, Michael P Coleman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

26 citing papers in PubMed, 36 citations in OpenAlex.

  1. Review
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  13. SARM1 can be a potential therapeutic target for spinal cord injury.Cellular and molecular life sciences : CMLS · 2022
    Review
  14. Protein Lipidation by Palmitoylation and Myristoylation in Cancer.Frontiers in cell and developmental biology · 2021
    Review
  15. Protein S-Palmitoylation and Lung Diseases.Advances in experimental medicine and biology · 2021
    Article
  16. Article
  17. Review
  18. Palmitoylation enables MAPK-dependent proteostasis of axon survival factors.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Review
  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

2 authors at 1 institution in 1 country.

Stefan MildeFrom the Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, United Kingdom.
Michael P ColemanFrom the Babraham Institute, Babraham Research Campus, Cambridge CB22 3AT, United Kingdom michael.coleman@babraham.ac.uk.
Babraham Institute · GB

Funding

Biotechnology and Biological Sciences Research Council BBS/E/B/0000M739Biotechnology and Biological Sciences Research Council BBS/E/B/000C0417Medical Research Council
6 · The paper itself

Abstract

The NAD-synthesizing enzyme nicotinamide mononucleotide adenylyltransferase 2 (NMNAT2) is a critical survival factor for axons and its constant supply from neuronal cell bodies into axons is required for axon survival in primary culture neurites and axon extension in vivo. Recently, we showed that palmitoylation is necessary to target NMNAT2 to post-Golgi vesicles, thereby influencing its protein turnover and axon protective capacity. Here we find that NMNAT2 is a substrate for cytosolic thioesterases APT1 and APT2 and that palmitoylation/depalmitoylation dynamics are on a time scale similar to its short half-life. Interestingly, however, depalmitoylation does not release NMNAT2 from membranes. The mechanism of palmitoylation-independent membrane attachment appears to be mediated by the same minimal domain required for palmitoylation itself. Furthermore, we identify several zDHHC palmitoyltransferases that influence NMNAT2 palmitoylation and subcellular localization, among which a role for zDHHC17 (HIP14) in neuronal NMNAT2 palmitoylation is best supported by our data. These findings shed light on the enzymatic regulation of NMNAT2 palmitoylation and highlight individual thioesterases and palmitoyltransferases as potential targets to modulate NMNAT2-dependent axon survival.

Indexed as

AcyltransferasesAnimalsAxonsBlotting, WesternCell MembraneCells, CulturedHEK293 CellsHumansLipoylationMice, Inbred C57BLMutationNeuronsNicotinamide-Nucleotide AdenylyltransferasePalmitic AcidPropiolactoneReverse Transcriptase Polymerase Chain ReactionAcyltransferasesLypla1 protein, mouseLypla2 protein, mouseNicotinamide-Nucleotide AdenylyltransferaseNmnat2 protein, mousePalmitic Acidpalmostatin BPropiolactoneThiolester HydrolasesZdhhc17 protein, mouseAPT1APT2EnzymeIntracellular TraffickingNeurodegenerationNMNAT2PalmitoyltransferaseProtein AcylationProtein PalmitoylationzDHHC17

Identifiers

PMID25271157
PMCPMC4239634
OpenAlexW2077132455

What OpenQuestion holds

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LicenceCC BY
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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.