Evidence map›Paper›PMID 9707576›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

A putative vacuolar cargo receptor partially colocalizes with AtPEP12p on a prevacuolar compartment in Arabidopsis roots.

A A Sanderfoot, S U Ahmed, D Marty-Mazars, I Rapoport, T Kirchhausen, F Marty, N V Raikhel

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.

0numbers the graph read from it
0cells of the map it votes in
76citing papers in PubMed
5.1field-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

76 citing papers in PubMed, 172 citations in OpenAlex.

  1. Review
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  3. MTV proteins unveil ER- and microtubule-associated compartments in the plant vacuolar trafficking pathway.Proceedings of the National Academy of Sciences of the United States of America · 2020
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16 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

7 authors at 3 institutions in 2 countries.

A A SanderfootMichigan State University-Department of Energy Plant Research Laboratory, Michigan State University, East Lansing, MI 48824, USA.
S U Ahmed
D Marty-Mazars
I Rapoport
T Kirchhausen
F Marty
N V Raikhel
Michigan State University · USHarvard University · USUniversité de Bourgogne · FR

Funding

STRUCTURAL CHEMISTRY OF CLATHRIN &ASSOCIATED PROTEINSR01GM036548 · NIGMS · IMMUNE DISEASE INSTITUTE, INC. · PI KIRCHHAUSEN, TOMAS · 1986 to 2014
$9.8M
ACTPEP12 AND VACUOLAR TARGETINGF32GM018861 · NIGMS · MICHIGAN STATE UNIVERSITY · PI SANDERFOOT, ANTON A · 1997 to 1999
–
NIGMS NIH HHS F32 GM018861NIGMS NIH HHS GM18861NIGMS NIH HHS GM36548NIGMS NIH HHS R01 GM036548
6 · The paper itself

Abstract

Targeting of protein cargo to the vacuole/lysosome is a multistep process that appears to have conserved features between mammalian, yeast, and plant cells. In each case, some soluble vacuolar/lysosomal proteins are believed to be bound by transmembrane cargo receptors in the trans-Golgi network (TGN) that redirect these proteins into clathrin-coated vesicles. These vesicles then appear to be transported to the prevacuole/endosome by a trafficking machinery that requires components identified in other vesicle-targeting steps such as N-ethylmaleimide-sensitive factor (NSF), soluble NSF attachment protein (SNAP), SNAP receptors (SNAREs), rab-type GTPases, and Sec1p homologs. Two likely members of this trafficking machinery have been characterized from Arabidopsis thaliana: AtPEP12p, a t-SNARE that resides on a what we now call a prevacuolar compartment, and AtELP, a protein that shares many common features with mammalian and yeast transmembrane cargo receptors. Here, we have further investigated the intracellular distribution of AtELP. We have found that AtELP is located at the trans-Golgi of Arabidopsis root cells, and that its C terminus can preferentially interact in vitro with the mammalian TGN-specific AP-1 clathrin-adapter complex, suggesting a likely role in clathrin-coated, vesicle-directed trafficking at the TGN. Further, consistent with a role in trafficking of vacuolar cargo, we have found that AtELP partially colocalizes with AtPEP12p on a prevacuolar compartment.

Indexed as

Arabidopsis ProteinsAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportAnimalsArabidopsisBiological Transport, ActiveCell CompartmentationGolgi ApparatusIn Vitro TechniquesMembrane ProteinsMicroscopy, ImmunoelectronPlant ProteinsPlant RootsQa-SNARE ProteinsVacuolesAdaptor Protein Complex alpha SubunitsAdaptor Proteins, Vesicular TransportArabidopsis ProteinsATPEP12 protein, ArabidopsisELP protein, ArabidopsisMembrane ProteinsPlant ProteinsQa-SNARE Proteins

Identifiers

PMID9707576
PMCPMC21437
OpenAlexW2118318984

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.