Evidence map›Paper›PMID 27457955›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Crystal structure of a nuclear actin ternary complex.

Tingting Cao, Lingfei Sun, Yuxiang Jiang, Shanjin Huang, Jiawei Wang, Zhucheng Chen

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
4.2field-weighted citation impact, top 6% 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

29 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Envisioning a role for nuclear actin in prophase I spermatocytes.Frontiers in cell and developmental biology · 2023
    Review
  5. Structure of the NuA4 histone acetyltransferase complex.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Article
  7. Nuclear Actin Dynamics in Gene Expression, DNA Repair, and Cancer.Results and problems in cell differentiation · 2022
    Article
  8. Review
  9. Review
  10. Review
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. 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

6 authors at 1 institution in 1 country.

Tingting CaoMinistry of Education Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, P.R. China; School of Life Science, Tsinghua University, Beijing 100084, P.R. China;
Lingfei SunMinistry of Education Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, P.R. China; School of Life Science, Tsinghua University, Beijing 100084, P.R. China;
Yuxiang JiangSchool of Life Science, Tsinghua University, Beijing 100084, P.R. China;
Shanjin HuangSchool of Life Science, Tsinghua University, Beijing 100084, P.R. China;
Jiawei WangSchool of Life Science, Tsinghua University, Beijing 100084, P.R. China; State Key Laboratory of Bio-membrane and Membrane Biotechnology, Tsinghua University, Beijing 100086, P.R. China.
Zhucheng ChenMinistry of Education Key Laboratory of Protein Science, Tsinghua University, Beijing 100084, P.R. China; School of Life Science, Tsinghua University, Beijing 100084, P.R. China; zhucheng_chen@tsinghua.edu.cn.
Tsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin polymerizes and forms filamentous structures (F-actin) in the cytoplasm of eukaryotic cells. It also exists in the nucleus and regulates various nucleic acid transactions, particularly through its incorporation into multiple chromatin-remodeling complexes. However, the specific structure of actin and the mechanisms that regulate its polymeric nature inside the nucleus remain unknown. Here, we report the crystal structure of nuclear actin (N-actin) complexed with actin-related protein 4 (Arp4) and the helicase-SANT-associated (HSA) domain of the chromatin remodeler Swr1. The inner face and barbed end of N-actin are sequestered by interactions with Arp4 and the HSA domain, respectively, which prevents N-actin from polymerization and binding to many actin regulators. The two major domains of N-actin are more twisted than those of globular actin (G-actin), and its nucleotide-binding pocket is occluded, freeing N-actin from binding to and regulation by ATP. These findings revealed the salient structural features of N-actin that distinguish it from its cytoplasmic counterpart and provide a rational basis for its functions and regulation inside the nucleus.

Indexed as

ActinsAdenosine TriphosphateCell NucleusChromatin Assembly and DisassemblyChromosomal Proteins, Non-HistoneCrystallizationDNA-Binding ProteinsHEK293 CellsHeLa CellsHumansProtein DomainsActinsACTL6A protein, humanAdenosine TriphosphateChromosomal Proteins, Non-HistoneDNA-Binding ProteinsArp4chromatin remodelingcrystal structurenuclear actin

Identifiers

PMID27457955
PMCPMC4987789
OpenAlexW2492184771

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.