Evidence map›Paper›PMID 18032660›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2007

Drosophila huntingtin-interacting protein 14 is a presynaptic protein required for photoreceptor synaptic transmission and expression of the palmitoylated proteins synaptosome-associated protein 25 and cysteine string protein.

R Steven Stowers, Ehud Y Isacoff

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

39 citing papers in PubMed, 71 citations in OpenAlex.

  1. Review
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  11. AeLife · 2019
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  19. Role of manganese in neurodegenerative diseases.Journal of trace elements in medicine and biology : organ of the Society for Minerals and Trace Elements (GMS) · 2011
    Review
  20. Huntingtin-interacting protein 14 is a type 1 diabetes candidate protein regulating insulin secretion and beta-cell apoptosis.Proceedings of the National Academy of Sciences of the United States of America · 2011
    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.

R Steven StowersDepartment of Molecular and Cell Biology, University of California, Berkeley, Berkeley, California 94720, USA.
Ehud Y Isacoff
University of California, Berkeley · US

Funding

MOLECULAR BIOLOGY OF SYNAPTIC GROWTH AND PLASTICITYR01MH060711 · NIMH · UNIVERSITY OF CALIFORNIA BERKELEY · PI ISACOFF, EHUD · 2000 to 2004
$1.9M
Genetic Dissection of Synaptic TransmissionK01DA019458 · NIDA · UNIVERSITY OF CALIFORNIA BERKELEY · PI STOWERS, STEVE · 2005 to 2009
$573k
NIDA NIH HHS K01DA19458NIMH NIH HHS R01MH60711
6 · The paper itself

Abstract

Palmitoylation affects the trafficking, stability, aggregation, and/or functional activity of a substantial number of neuronal proteins. We identified mutations in dHIP14, the Drosophila homolog of the human palmitoyl transferase, Huntingtin-interacting protein 14 (HIP14). HIP14 was previously reported to localize primarily to Golgi and to palmitoylate the neuronal proteins synaptosome-associated protein 25 (SNAP-25), PSD-95 (postsynaptic density-95), GAD65, Synaptotagmin, and Huntingtin in mammalian neurons. We find dHIP14 to be an essential maternal effect gene required for photoreceptor synaptic transmission and for proper in vivo expression of the palmitoylated presynaptic proteins SNAP-25 and cysteine string protein. In non-neuronal cells in the fly, dHIP14 protein is found in Golgi. However, in fly neurons, we find dHIP14 primarily in presynaptic terminals, something we also observe with HIP14. In mammalian neurons, we also find a significant fraction of HIP14 colocalizing with a synaptic vesicle marker. Based on localization of the palmitoyl transferase HIP14 within the presynaptic nerve terminal, we propose palmitoylation as a possible mechanism that may be operating to rapidly regulate synaptic efficacy.

Indexed as

AcyltransferasesAdaptor Proteins, Signal TransducingAnimalsDrosophilaDrosophila ProteinsFemaleGene Expression RegulationLipoylationNerve Tissue ProteinsPhotoreceptor Cells, InvertebratePresynaptic TerminalsSynaptic TransmissionSynaptosomal-Associated Protein 25SynaptosomesAcyltransferasesAdaptor Proteins, Signal TransducingCsp protein, DrosophilaDrosophila ProteinsNerve Tissue ProteinsSNAP25 protein, humanSynaptosomal-Associated Protein 25ZDHHC17 protein, human

Identifiers

PMID18032660
PMCPMC6673277
OpenAlexW2014501341

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.