Evidence map›Paper›PMID 38134410›Full record

ArticleThe Plant cell2024

CHLOROPLAST UNUSUAL POSITIONING 1 is a plant-specific actin polymerization factor regulating chloroplast movement.

Sam-Geun Kong, Yosuke Yamazaki, Atsushi Shimada, Saku T Kijima, Keiko Hirose, Kaoru Katoh, Jeongsu Ahn, Hyun-Geun Song, Jae-Woo Han, Takeshi Higa and 6 more

Open access · greenAbstract read
In one paragraph

Article in The Plant cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
8.7field-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

16 citing papers in PubMed, 23 citations in OpenAlex.

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  7. Optimal disk packing of chloroplasts in plant cells.Proceedings of the National Academy of Sciences of the United States of America · 2025
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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

16 authors at 5 institutions in 2 countries.

Sam-Geun KongDepartment of Biological Sciences, College of Natural Sciences, Kongju National University, Chungnam 32588, Korea.ORCID 0000-0003-3013-4707
Yosuke YamazakiDepartment of Physics, Faculty of Science and Engineering, Waseda University, Tokyo 169-8555, Japan.ORCID 0000-0002-6863-3344
Atsushi ShimadaDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.ORCID 0000-0002-4108-770X
Saku T KijimaBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Ibaraki 305-8562, Japan.ORCID 0000-0003-1080-6289
Keiko HiroseBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Ibaraki 305-8562, Japan.ORCID 0000-0003-4587-8346
Kaoru KatohBiomedical Research Institute, National Institute of Advanced Industrial Science and Technology, Ibaraki 305-8562, Japan.ORCID 0000-0001-6590-413X
Jeongsu AhnDepartment of Biological Sciences, College of Natural Sciences, Kongju National University, Chungnam 32588, Korea.ORCID 0009-0009-7113-320X
Hyun-Geun SongDepartment of Biological Sciences, College of Natural Sciences, Kongju National University, Chungnam 32588, Korea.ORCID 0009-0002-4705-6151
Jae-Woo HanDepartment of Biological Sciences, College of Natural Sciences, Kongju National University, Chungnam 32588, Korea.ORCID 0009-0001-9004-1775
Takeshi HigaInstitute for Protein Research, Osaka University, Osaka 565-0871, Japan.ORCID 0000-0002-3196-2160
Akira TakanoDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.ORCID 0009-0000-8320-310X
Yuki NakamuraDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.ORCID 0009-0009-3794-0948
Noriyuki SuetsuguDepartment of Biology, Faculty of Sciences, Kyushu University, Fukuoka 812-8581, Japan.ORCID 0000-0002-3328-3313
Daisuke KohdaDivision of Structural Biology, Medical Institute of Bioregulation, Kyushu University, Fukuoka 812-8582, Japan.ORCID 0000-0001-8234-3776
Taro Q P UyedaDepartment of Physics, Faculty of Science and Engineering, Waseda University, Tokyo 169-8555, Japan.ORCID 0000-0002-3584-9499
Masamitsu WadaDepartment of Biology, Faculty of Sciences, Kyushu University, Fukuoka 812-8581, Japan.ORCID 0000-0001-6672-7411
Kyushu University · JPKongju National University · KRNational Institute of Advanced Industrial Science and Technology · JPWaseda University · JPProtein Research Foundation · JP

Funding

Basic Science Research Program through the National Research Foundation of KoreaJapan Society for the Promotion of Science 20227001Korea Innovation FoundationMinistry of Education 2021R1I1A3059996Ministry of Education, Culture, Sports, Science and Technology of JapanMinistry of Science and ICTNext-Generation Biogreen 21 ProgramOhsumi Frontier Science FoundationRural Development Administration
6 · The paper itself

Abstract

Plants have unique responses to fluctuating light conditions. One such response involves chloroplast photorelocation movement, which optimizes photosynthesis under weak light by the accumulation of chloroplasts along the periclinal side of the cell, which prevents photodamage under strong light by avoiding chloroplast positioning toward the anticlinal side of the cell. This light-responsive chloroplast movement relies on the reorganization of chloroplast actin (cp-actin) filaments. Previous studies have suggested that CHLOROPLAST UNUSUAL POSITIONING 1 (CHUP1) is essential for chloroplast photorelocation movement as a regulator of cp-actin filaments. In this study, we conducted comprehensive analyses to understand CHUP1 function. Functional, fluorescently tagged CHUP1 colocalized with and was coordinately reorganized with cp-actin filaments on the chloroplast outer envelope during chloroplast movement in Arabidopsis thaliana. CHUP1 distribution was reversibly regulated in a blue light- and phototropin-dependent manner. X-ray crystallography revealed that the CHUP1-C-terminal domain shares structural homology with the formin homology 2 (FH2) domain, despite lacking sequence similarity. Furthermore, the CHUP1-C-terminal domain promoted actin polymerization in the presence of profilin in vitro. Taken together, our findings indicate that CHUP1 is a plant-specific actin polymerization factor that has convergently evolved to assemble cp-actin filaments and enables chloroplast photorelocation movement.

Indexed as

ArabidopsisArabidopsis ProteinsActin CytoskeletonActinsChloroplast ProteinsChloroplastsLightMovementPolymerizationActinsArabidopsis ProteinsChloroplast Proteins

Identifiers

PMID38134410
PMCPMC10980345
OpenAlexW4390099315

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.