Evidence map›Paper›PMID 24280388›Full record

ArticleThe Plant cell2013

MAIGO5 functions in protein export from Golgi-associated endoplasmic reticulum exit sites in Arabidopsis.

Junpei Takagi, Luciana Renna, Hideyuki Takahashi, Yasuko Koumoto, Kentaro Tamura, Giovanni Stefano, Yoichiro Fukao, Maki Kondo, Mikio Nishimura, Tomoo Shimada and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
2.8field-weighted citation impact, top 10% 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

33 citing papers in PubMed, 61 citations in OpenAlex.

  1. Emerging roles of non-mNature plants · 2026
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  5. Article
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  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. On the nature of the plant ER exit sites.Frontiers in plant science · 2022
    Article
  13. A unique AtSar1D-AtRabD2a nexus modulates autophagosome biogenesis inProceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  14. Article
  15. TALEN-BasedFrontiers in plant science · 2021
    Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. A Model for ERD2 Function in Higher Plants.Frontiers in plant science · 2020
    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

12 authors at 4 institutions in 2 countries.

Junpei TakagiDepartment of Botany, Graduate School of Science, Kyoto University, Sakyo-ku, Kyoto 606-8502, Japan.
Luciana Renna
Hideyuki Takahashi
Yasuko Koumoto
Kentaro Tamura
Giovanni Stefano
Yoichiro Fukao
Maki Kondo
Mikio Nishimura
Tomoo Shimada
Federica Brandizzi
Ikuko Hara-Nishimura
Kyoto University · JPMichigan State University · USNational Institute for Basic Biology · JPNara Institute of Science and Technology · JP

Funding

Unfolded protein response in the model species Arabidopsis thalianaR01GM101038 · NIGMS · MICHIGAN STATE UNIVERSITY · PI BRANDIZZI, FEDERICA · 2012 to 2019
$2.5M
NIGMS NIH HHS R01 GM101038NIGMS NIH HHS R01 GM101038-01
6 · The paper itself

Abstract

Plant cells face unique challenges to efficiently export cargo from the endoplasmic reticulum (ER) to mobile Golgi stacks. Coat protein complex II (COPII) components, which include two heterodimers of Secretory23/24 (Sec23/24) and Sec13/31, facilitate selective cargo export from the ER; however, little is known about the mechanisms that regulate their recruitment to the ER membrane, especially in plants. Here, we report a protein transport mutant of Arabidopsis thaliana, named maigo5 (mag5), which abnormally accumulates precursor forms of storage proteins in seeds. mag5-1 has a deletion in the putative ortholog of the Saccharomyces cerevisiae and Homo sapiens Sec16, which encodes a critical component of ER exit sites (ERESs). mag mutants developed abnormal structures (MAG bodies) within the ER and exhibited compromised ER export. A functional MAG5/SEC16A-green fluorescent protein fusion localized at Golgi-associated cup-shaped ERESs and cycled on and off these sites at a slower rate than the COPII coat. MAG5/SEC16A interacted with SEC13 and SEC31; however, in the absence of MAG5/SEC16A, recruitment of the COPII coat to ERESs was accelerated. Our results identify a key component of ER export in plants by demonstrating that MAG5/SEC16A is required for protein export at ERESs that are associated with mobile Golgi stacks, where it regulates COPII coat turnover.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsEndoplasmic ReticulumGolgi ApparatusGreen Fluorescent ProteinsMolecular Sequence DataMutationPlants, Genetically ModifiedProtein TransportRecombinant Fusion ProteinsSeedsSequence Homology, Amino AcidVesicular Transport ProteinsArabidopsis ProteinsGreen Fluorescent ProteinsRecombinant Fusion ProteinsSEC16A protein, humanSEC24 protein, ArabidopsisVesicular Transport Proteins

Identifiers

PMID24280388
PMCPMC3875742
OpenAlexW2135841395

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.