Evidence map›Paper›PMID 23733933›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2013

Arabidopsis μ-adaptin subunit AP1M of adaptor protein complex 1 mediates late secretory and vacuolar traffic and is required for growth.

Misoon Park, Kyungyoung Song, Ilka Reichardt, Hyeran Kim, Ulrike Mayer, York-Dieter Stierhof, Inhwan Hwang, Gerd Jürgens

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

80 citing papers in PubMed, 148 citations in OpenAlex.

  1. Article
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  5. Article
  6. Cargo Sorting Zones in Plant Trans-Golgi Network.Sub-cellular biochemistry · 2026
    Review
  7. Post-Golgi Trafficking in Plant Cells.Sub-cellular biochemistry · 2026
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. An Overview of Protein Secretion in Plant Cells.Methods in molecular biology (Clifton, N.J.) · 2024
    Review
  17. Article
  18. Article
  19. Article
  20. FgAP1Journal of fungi (Basel, Switzerland) · 2023
    Article

20 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

8 authors at 2 institutions in 2 countries.

Misoon ParkEntwicklungsgenetik and Microscopy, Zentrum für Molekularbiologie der Pflanzen (ZMBP), University of Tübingen, 72076 Tübingen, Germany.
Kyungyoung Song
Ilka Reichardt
Hyeran Kim
Ulrike Mayer
York-Dieter Stierhof
Inhwan Hwang
Gerd Jürgens
Pohang University of Science and Technology · KRUniversity of Tübingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Adaptor protein (AP) complexes are the predominant coat proteins of membrane vesicles in post-Golgi trafficking of mammalian cells. Each AP complex contains a specific medium subunit, μ-adaptin, that selects cargo proteins bearing sequence-specific sorting motifs. Much less is known about the AP complexes and their μ subunits in plants. Because of uncertain homology, the μ-adaptins of Arabidopsis have been designated muA through muD [Happel et al. (2004) Plant J 37(5):678-693]. Furthermore, only muD has been assigned to a specific AP complex, AP-3, involved in Golgi-vacuolar trafficking [Niihama et al. (2009) Plant Cell Physiol 50(12):2057-2068, Zwiewka et al. (2011) Cell Res 21(12):1711-1722, and Wolfenstetter et al. (2012) Plant Cell 24(1):215-232]. In contrast, the μ subunit of neither the post-Golgi trafficking AP-1 complex nor the endocytic AP-2 complex has been identified. Here, we report the functional analysis of redundant AP-1 μ-adaptins AP1M1 (also known as muB1) and AP1M2 (also known as muB2). Coimmunoprecipitation revealed that both AP1M2 and its less strongly expressed isoform AP1M1 are complexed with the large subunit γ-adaptin of AP-1. In addition, AP1M2 was localized at or near the trans-Golgi network. Knockout mutations of AP1M2 impaired pollen function and arrested plant growth whereas the ap1m1 ap1m2 double mutant was nearly pollen-lethal. At the cellular level, the absence of AP1M2 entailed inhibition of multiple trafficking pathways from the trans-Golgi network to the vacuole and to the plasma membrane in interphase and to the plane of cell division in cytokinesis. Thus, AP-1 is crucial in post-Golgi trafficking in plant cells and required for cell division and plant growth.

Indexed as

Adaptor Protein Complex 1Adaptor Protein Complex alpha SubunitsAdaptor Protein Complex gamma SubunitsAdaptor Protein Complex mu SubunitsArabidopsisArabidopsis ProteinsCell MembraneCytokinesisGolgi ApparatusInterphaseMicroscopy, Electron, TransmissionMutagenesis, InsertionalProtein TransportSecretory Vesiclestrans-Golgi NetworkVacuolesAdaptor Protein Complex 1adaptor protein complex 1, mu 1 subunitadaptor protein complex 1, mu 2 subunitAdaptor Protein Complex alpha SubunitsAdaptor Protein Complex gamma SubunitsAdaptor Protein Complex mu SubunitsAP1M1 protein, ArabidopsisAP1M2 protein, ArabidopsisArabidopsis Proteinsadaptor complex 1developmentmembrane trafficsecretory pathway

Identifiers

PMID23733933
PMCPMC3690844
OpenAlexW1991082293

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.