Evidence map›Paper›PMID 27261463›Full record

ArticleThe Journal of biological chemistry2016

The Structurally Plastic CH2 Domain Is Linked to Distinct Functions of Fimbrins/Plastins.

Ruihui Zhang, Ming Chang, Meng Zhang, Youjun Wu, Xiaolu Qu, Shanjin Huang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.3field-weighted citation impact, top 14% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Trial
  2. Review
  3. Article
  4. Article
  5. Review
  6. Review
  7. Plastin 3 in health and disease: a matter of balance.Cellular and molecular life sciences : CMLS · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Actin Bundles in The Pollen Tube.International journal of molecular sciences · 2018
    Review
  12. Article
  13. Article
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

6 authors at 2 institutions in 2 countries.

Ruihui ZhangFrom the Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, the University of Chinese Academy of Sciences, Beijing 100049, China.
Ming Changthe Center for Plant Biology, School of Life Sciences, Tsinghua University, Beijing 100084.
Meng ZhangFrom the Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, the University of Chinese Academy of Sciences, Beijing 100049, China.
Youjun WuFrom the Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093.
Xiaolu Quthe Center for Plant Biology, School of Life Sciences, Tsinghua University, Beijing 100084, the Tsinghua-Peking Joint Center for Life Sciences, Beijing 100084, and.
Shanjin HuangFrom the Key Laboratory of Plant Molecular Physiology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, the Center for Plant Biology, School of Life Sciences, Tsinghua University, Beijing 100084, sjhuang@tsinghua.edu.cn.ORCID 0000-0001-9517-2515
Chinese Academy of Sciences · CNCenter for Life Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fimbrins/plastins have been implicated in the generation of distinct actin structures, which are linked to different cellular processes. Historically, fimbrins/plastins were mainly considered as generating tight actin bundles. Here, we demonstrate that different members of the fimbrin/plastin family have diverged biochemically during evolution to generate either tight actin bundles or loose networks with distinct biochemical and biophysical properties. Using the phylogenetically and functionally distinct Arabidopsis fimbrins FIM4 and FIM5 we found that FIM4 generates both actin bundles and cross-linked actin filaments, whereas FIM5 only generates actin bundles. The distinct functions of FIM4 and FIM5 are clearly observed at single-filament resolution. Domain swapping experiments showed that cooperation between the conformationally plastic calponin-homology domain 2 (CH2) and the N-terminal headpiece determines the function of the full-length protein. Our study suggests that the structural plasticity of fimbrins/plastins has biologically meaningful consequences, and provides novel insights into the structure-function relationship of fimbrins/plastins as well as shedding light on how cells generate distinct actin structures.

Indexed as

Actin CytoskeletonAnimalsArabidopsisArabidopsis ProteinsMembrane GlycoproteinsMiceMicrofilament ProteinsProtein DomainsArabidopsis ProteinsMembrane GlycoproteinsMicrofilament ProteinsplastinactinArabidopsisArp2/3 complexcytoskeletonmicrofilamentsplant

Identifiers

PMID27261463
PMCPMC5016177
OpenAlexW2409996219

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.