Evidence map›Paper›PMID 26546666›Full record

ArticlePlant physiology2016

The Adaptor Complex AP-4 Regulates Vacuolar Protein Sorting at the trans-Golgi Network by Interacting with VACUOLAR SORTING RECEPTOR1.

Kentaro Fuji, Makoto Shirakawa, Yuki Shimono, Tadashi Kunieda, Yoichiro Fukao, Yasuko Koumoto, Hideyuki Takahashi, Ikuko Hara-Nishimura, Tomoo Shimada

Open access · greenAbstract read
In one paragraph

Article in Plant physiology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

42 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
  2. Article
  3. Cargo Sorting Zones in Plant Trans-Golgi Network.Sub-cellular biochemistry · 2026
    Review
  4. Post-Golgi Trafficking in Plant Cells.Sub-cellular biochemistry · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Vesicle trafficking in rice: too little is known.Frontiers in plant science · 2023
    Review
  15. Article
  16. Review
  17. Article
  18. Review
  19. The sorting of cargo proteins in the plantFrontiers in plant science · 2022
    Review
  20. Review
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

9 authors at 1 institution in 1 country.

Kentaro FujiGraduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan (K.F., M.S., Y.S., T.K., Y.K., H.T., I.H.-N., T.S.); andPlant Global Educational Project, Nara Institute of Science and Technology, Ikoma 630-0192, Japan (Y.F.).
Makoto ShirakawaGraduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan (K.F., M.S., Y.S., T.K., Y.K., H.T., I.H.-N., T.S.); andPlant Global Educational Project, Nara Institute of Science and Technology, Ikoma 630-0192, Japan (Y.F.).
Yuki ShimonoGraduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan (K.F., M.S., Y.S., T.K., Y.K., H.T., I.H.-N., T.S.); andPlant Global Educational Project, Nara Institute of Science and Technology, Ikoma 630-0192, Japan (Y.F.).
Tadashi KuniedaGraduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan (K.F., M.S., Y.S., T.K., Y.K., H.T., I.H.-N., T.S.); andPlant Global Educational Project, Nara Institute of Science and Technology, Ikoma 630-0192, Japan (Y.F.).
Yoichiro FukaoGraduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan (K.F., M.S., Y.S., T.K., Y.K., H.T., I.H.-N., T.S.); andPlant Global Educational Project, Nara Institute of Science and Technology, Ikoma 630-0192, Japan (Y.F.).
Yasuko KoumotoGraduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan (K.F., M.S., Y.S., T.K., Y.K., H.T., I.H.-N., T.S.); andPlant Global Educational Project, Nara Institute of Science and Technology, Ikoma 630-0192, Japan (Y.F.).
Hideyuki TakahashiGraduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan (K.F., M.S., Y.S., T.K., Y.K., H.T., I.H.-N., T.S.); andPlant Global Educational Project, Nara Institute of Science and Technology, Ikoma 630-0192, Japan (Y.F.).
Ikuko Hara-NishimuraGraduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan (K.F., M.S., Y.S., T.K., Y.K., H.T., I.H.-N., T.S.); andPlant Global Educational Project, Nara Institute of Science and Technology, Ikoma 630-0192, Japan (Y.F.) ihnishi@gr.bot.kyoto-u.ac.jp tshimada@gr.bot.kyoto-u.ac.jp.ORCID http://orcid.org/0000-0001-8814-1593
Tomoo ShimadaGraduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan (K.F., M.S., Y.S., T.K., Y.K., H.T., I.H.-N., T.S.); andPlant Global Educational Project, Nara Institute of Science and Technology, Ikoma 630-0192, Japan (Y.F.) ihnishi@gr.bot.kyoto-u.ac.jp tshimada@gr.bot.kyoto-u.ac.jp.
Kyoto University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adaptor protein (AP) complexes play critical roles in protein sorting among different post-Golgi pathways by recognizing specific cargo protein motifs. Among the five AP complexes (AP-1-AP-5) in plants, AP-4 is one of the most poorly understood; the AP-4 components, AP-4 cargo motifs, and AP-4 functional mechanism are not known. Here, we identify the AP-4 components and show that the AP-4 complex regulates receptor-mediated vacuolar protein sorting by recognizing VACUOLAR SORTING RECEPTOR1 (VSR1), which was originally identified as a sorting receptor for seed storage proteins to target protein storage vacuoles in Arabidopsis (Arabidopsis thaliana). From the vacuolar sorting mutant library GREEN FLUORESCENT SEED (GFS), we isolated three gfs mutants that accumulate abnormally high levels of VSR1 in seeds and designated them as gfs4, gfs5, and gfs6. Their responsible genes encode three (AP4B, AP4M, and AP4S) of the four subunits of the AP-4 complex, respectively, and an Arabidopsis mutant (ap4e) lacking the fourth subunit, AP4E, also had the same phenotype. Mass spectrometry demonstrated that these four proteins form a complex in vivo. The four mutants showed defects in the vacuolar sorting of the major storage protein 12S globulins, indicating a role for the AP-4 complex in vacuolar protein transport. AP4M bound to the tyrosine-based motif of VSR1. AP4M localized at the trans-Golgi network (TGN) subdomain that is distinct from the AP-1-localized TGN subdomain. This study provides a novel function for the AP-4 complex in VSR1-mediated vacuolar protein sorting at the specialized domain of the TGN.

Indexed as

Adaptor Protein Complex 4Amino Acid MotifsArabidopsisArabidopsis ProteinsGreen Fluorescent ProteinsMutationPlants, Genetically ModifiedProtein TransportSeedstrans-Golgi NetworkVacuolesAdaptor Protein Complex 4Arabidopsis ProteinsELP protein, ArabidopsisGreen Fluorescent Proteins

Identifiers

PMID26546666
PMCPMC4704568
OpenAlexW2205957564

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.