Evidence map›Paper›PMID 23804088›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2013

Multiple dileucine-like motifs direct VGLUT1 trafficking.

Sarah M Foss, Haiyan Li, Magda S Santos, Robert H Edwards, Susan M Voglmaier

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
2.8field-weighted citation impact, top 11% 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

37 citing papers in PubMed, 54 citations in OpenAlex.

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  9. Vesicular neurotransmitter transporters in Drosophila melanogaster.Biochimica et biophysica acta. Biomembranes · 2020
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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 2 institutions in 1 country.

Sarah M FossDepartments of Psychiatry, Neurology, and Physiology, and Graduate Program in Cell Biology, School of Medicine, University of California, San Francisco, San Francisco, California 94143-0984, USA.
Haiyan Li
Magda S Santos
Robert H Edwards
Susan M Voglmaier
Neurology, Inc · USUniversity of California, San Francisco · US

Funding

The Presynaptic Vesicle Cycle for the Slow Acting Neurotransmitter SecretionP01DA010154 · NIDA · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI KREITZER, ANATOL, SULZER, DAVID · 1995 to 2016
$14.7M
Membrane Trafficking of Vesicular Neurotransmitter TransportersR01MH083691 · NIMH · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI VOGLMAIER, SUSAN M. · 2011 to 2022
$3.9M
NIDA NIH HHS P01 DA010154NIMH NIH HHS R01 MH083691
6 · The paper itself

Abstract

The vesicular glutamate transporters (VGLUTs) package glutamate into synaptic vesicles, and the two principal isoforms VGLUT1 and VGLUT2 have been suggested to influence the properties of release. To understand how a VGLUT isoform might influence transmitter release, we have studied their trafficking and previously identified a dileucine-like endocytic motif in the C terminus of VGLUT1. Disruption of this motif impairs the activity-dependent recycling of VGLUT1, but does not eliminate its endocytosis. We now report the identification of two additional dileucine-like motifs in the N terminus of VGLUT1 that are not well conserved in the other isoforms. In the absence of all three motifs, rat VGLUT1 shows limited accumulation at synaptic sites and no longer responds to stimulation. In addition, shRNA-mediated knockdown of clathrin adaptor proteins AP-1 and AP-2 shows that the C-terminal motif acts largely via AP-2, whereas the N-terminal motifs use AP-1. Without the C-terminal motif, knockdown of AP-1 reduces the proportion of VGLUT1 that responds to stimulation. VGLUT1 thus contains multiple sorting signals that engage distinct trafficking mechanisms. In contrast to VGLUT1, the trafficking of VGLUT2 depends almost entirely on the conserved C-terminal dileucine-like motif: without this motif, a substantial fraction of VGLUT2 redistributes to the plasma membrane and the transporter's synaptic localization is disrupted. Consistent with these differences in trafficking signals, wild-type VGLUT1 and VGLUT2 differ in their response to stimulation.

Indexed as

Adaptor Protein Complex 2Amino Acid MotifsAmino Acid SequenceAnimalsCells, CulturedClathrinEndocytosisHippocampusHydrogen-Ion ConcentrationImmunohistochemistryLeucineMolecular Sequence DataMutant Chimeric ProteinsPolymerase Chain ReactionRatsRNA InterferenceAdaptor Protein Complex 2ClathrinLeucineMutant Chimeric ProteinsSlc17a6 protein, ratSlc17a7 protein, ratVesicular Glutamate Transport Protein 1Vesicular Glutamate Transport Protein 2

Identifiers

PMID23804088
PMCPMC3693054
OpenAlexW1975802967

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.