Evidence map›Paper›PMID 23715471›Full record

ArticleThe Plant cell2013

Chloroplast division protein ARC3 regulates chloroplast FtsZ-ring assembly and positioning in arabidopsis through interaction with FtsZ2.

Min Zhang, Aaron J Schmitz, Deena K Kadirjan-Kalbach, Allan D Terbush, Katherine W Osteryoung

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 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.4field-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

34 citing papers in PubMed, 54 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Enhanced chloroplast FtsZ-ring constriction by the ARC6-ARC3 module inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  5. Article
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  8. Article
  9. Structural and functional insights into the chloroplast division site regulators PARC6 and PDV1 in the intermembrane space.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  10. What can hornworts teach us?Frontiers in plant science · 2023
    Review
  11. Article
  12. Article
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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 1 institution in 1 country.

Min ZhangDepartment of Plant Biology, Michigan State University, East Lansing, Michigan 48824, USA.
Aaron J Schmitz
Deena K Kadirjan-Kalbach
Allan D Terbush
Katherine W Osteryoung
Michigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chloroplast division is initiated by assembly of a mid-chloroplast FtsZ (Z) ring comprising two cytoskeletal proteins, FtsZ1 and FtsZ2. The division-site regulators ACCUMULATION AND REPLICATION OF CHLOROPLASTS3 (ARC3), MinD1, and MinE1 restrict division to the mid-plastid, but their roles are poorly understood. Using genetic analyses in Arabidopsis thaliana, we show that ARC3 mediates division-site placement by inhibiting Z-ring assembly, and MinD1 and MinE1 function through ARC3. ftsZ1 null mutants exhibited some mid-plastid FtsZ2 rings and constrictions, whereas neither constrictions nor FtsZ1 rings were observed in mutants lacking FtsZ2, suggesting FtsZ2 is the primary determinant of Z-ring assembly in vivo. arc3 ftsZ1 double mutants exhibited multiple parallel but no mid-plastid FtsZ2 rings, resembling the Z-ring phenotype in arc3 single mutants and showing that ARC3 affects positioning of FtsZ2 rings as well as Z rings. ARC3 overexpression in the wild type and ftsZ1 inhibited Z-ring and FtsZ2-ring assembly, respectively. Consistent with its effects in vivo, ARC3 interacted with FtsZ2 in two-hybrid assays and inhibited FtsZ2 assembly in a heterologous system. Our studies are consistent with a model wherein ARC3 directly inhibits Z-ring assembly in vivo primarily through interaction with FtsZ2 in heteropolymers and suggest that ARC3 activity is spatially regulated by MinD1 and MinE1 to permit Z-ring assembly at the mid-plastid.

Indexed as

Adenosine TriphosphatasesArabidopsisArabidopsis ProteinsCell Cycle ProteinsChloroplastsImmunoblottingMicroscopy, FluorescenceMutationPlants, Genetically ModifiedPolymerizationProtein BindingTwo-Hybrid System TechniquesAdenosine TriphosphatasesArabidopsis ProteinsARC3 protein, ArabidopsisCell Cycle ProteinsFtsZ1 protein, ArabidopsisFTSZ protein, ArabidopsisMinD1 protein, ArabidopsisMinE1 protein, Arabidopsis

Identifiers

PMID23715471
PMCPMC3694706
OpenAlexW2171289092

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.