Evidence map›Paper›PMID 26527658›Full record

ArticlePlant physiology2016

Roles of Arabidopsis PARC6 in Coordination of the Chloroplast Division Complex and Negative Regulation of FtsZ Assembly.

Min Zhang, Cheng Chen, John E Froehlich, Allan D TerBush, Katherine W Osteryoung

Abstract 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 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
–field-weighted citation impact
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

25 citing papers in PubMed.

  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. Review
  6. Article
  7. Article
  8. 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
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Frontiers in plant science · 2019
    Article
  16. Article
  17. Article
  18. Insights into the Mechanisms of Chloroplast Division.International journal of molecular sciences · 2018
    Review
  19. 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

5 authors.

Min ZhangDepartment of Plant Biology (M.Z., C.C., A.D.T., K.W.O.), Michigan State University-Department of Energy Plant Research Laboratory (J.E.F.), and Department of Biochemistry and Molecular Biology (J.E.F.), Michigan State University, East Lansing, Michigan 48824; andCollege of Life Sciences, Capital Normal University, Beijing 100048, China (M.Z.).ORCID http://orcid.org/0000-0002-3716-4565
Cheng ChenDepartment of Plant Biology (M.Z., C.C., A.D.T., K.W.O.), Michigan State University-Department of Energy Plant Research Laboratory (J.E.F.), and Department of Biochemistry and Molecular Biology (J.E.F.), Michigan State University, East Lansing, Michigan 48824; andCollege of Life Sciences, Capital Normal University, Beijing 100048, China (M.Z.).
John E FroehlichDepartment of Plant Biology (M.Z., C.C., A.D.T., K.W.O.), Michigan State University-Department of Energy Plant Research Laboratory (J.E.F.), and Department of Biochemistry and Molecular Biology (J.E.F.), Michigan State University, East Lansing, Michigan 48824; andCollege of Life Sciences, Capital Normal University, Beijing 100048, China (M.Z.).
Allan D TerBushDepartment of Plant Biology (M.Z., C.C., A.D.T., K.W.O.), Michigan State University-Department of Energy Plant Research Laboratory (J.E.F.), and Department of Biochemistry and Molecular Biology (J.E.F.), Michigan State University, East Lansing, Michigan 48824; andCollege of Life Sciences, Capital Normal University, Beijing 100048, China (M.Z.).
Katherine W OsteryoungDepartment of Plant Biology (M.Z., C.C., A.D.T., K.W.O.), Michigan State University-Department of Energy Plant Research Laboratory (J.E.F.), and Department of Biochemistry and Molecular Biology (J.E.F.), Michigan State University, East Lansing, Michigan 48824; andCollege of Life Sciences, Capital Normal University, Beijing 100048, China (M.Z.) osteryou@msu.edu.ORCID http://orcid.org/0000-0002-0028-2509

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Chloroplast division is driven by the simultaneous constriction of the inner FtsZ ring (Z ring) and the outer DRP5B ring. The assembly and constriction of these rings in Arabidopsis (Arabidopsis thaliana) are coordinated partly through the inner envelope membrane protein ACCUMULATION AND REPLICATION OF CHLOROPLASTS6 (ARC6). Previously, we showed that PARC6 (PARALOG OF ARC6), also in the inner envelope membrane, negatively regulates FtsZ assembly and acts downstream of ARC6 to position the outer envelope membrane protein PLASTID DIVISION1 (PDV1), which functions together with its paralog PDV2 to recruit DYNAMIN-RELATED PROTEIN 5B (DRP5B) from a cytosolic pool to the outer envelope membrane. However, whether PARC6, like ARC6, also functions in coordination of the chloroplast division contractile complexes was unknown. Here, we report a detailed topological analysis of Arabidopsis PARC6, which shows that PARC6 has a single transmembrane domain and a topology resembling that of ARC6. The newly identified stromal region of PARC6 interacts not only with ARC3, a direct inhibitor of Z-ring assembly, but also with the Z-ring protein FtsZ2. Overexpression of PARC6 inhibits FtsZ assembly in Arabidopsis but not in a heterologous yeast system (Schizosaccharomyces pombe), suggesting that the negative regulation of FtsZ assembly by PARC6 is a consequence of its interaction with ARC3. A conserved carboxyl-terminal peptide in FtsZ2 mediates FtsZ2 interaction with both PARC6 and ARC6. Consistent with its role in the positioning of PDV1, the intermembrane space regions of PARC6 and PDV1 interact. These findings provide new insights into the functions of PARC6 and suggest that PARC6 coordinates the inner Z ring and outer DRP5B ring through interaction with FtsZ2 and PDV1 during chloroplast division.

Indexed as

ArabidopsisArabidopsis ProteinsCell MembraneChloroplastsDynaminsGene Expression Regulation, PlantPlants, Genetically ModifiedProtein Interaction MappingProtein Structure, TertiaryArabidopsis ProteinsARC3 protein, ArabidopsisARC5 protein, ArabidopsisARC6 protein, ArabidopsisDynaminsFTSZ protein, ArabidopsisPARC6 protein, Arabidopsisplastid division protein PDV1, Arabidopsis

Identifiers

PMID26527658
PMCPMC4704591

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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.