Evidence map›Paper›PMID 28841137›Full record

ArticleeLife2017

Autoinhibition of ankyrin-B/G membrane target bindings by intrinsically disordered segments from the tail regions.

Keyu Chen, Jianchao Li, Chao Wang, Zhiyi Wei, Mingjie Zhang

Open access · goldAbstract read
In one paragraph

Article in eLife, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.9field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Connecting sequence features within the disordered C-terminal linker ofProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  6. Architecture of the human erythrocyte ankyrin-1 complex.Nature structural & molecular biology · 2022
    Article
  7. Article
  8. Review
  9. A Rare Variant ofFrontiers in neurology · 2021
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. An unfolding role for ankyrin-G at the axon initial segment.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Neurodevelopmental mutation of giant ankyrin-G disrupts a core mechanism for axon initial segment assembly.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  16. Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  17. Ankyrins: Roles in synaptic biology and pathology.Molecular and cellular neurosciences · 2018
    Review
  18. 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

5 authors at 2 institutions in 2 countries.

Keyu Chen *Division of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Hong Kong, China.ORCID http://orcid.org/0000-0003-0321-0604
Jianchao Li *Division of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Hong Kong, China.ORCID http://orcid.org/0000-0002-8921-1626
Chao WangDivision of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Hong Kong, China.
Zhiyi WeiDivision of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Hong Kong, China.ORCID http://orcid.org/0000-0002-4446-6502
Mingjie ZhangDivision of Life Science, State Key Laboratory of Molecular Neuroscience, Hong Kong University of Science and Technology, Hong Kong, China.ORCID http://orcid.org/0000-0001-9404-0190
Hong Kong University of Science and Technology · HKUniversity of Science and Technology of China · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Ankyrins together with their spectrin partners are the master organizers of micron-scale membrane domains in diverse tissues. The 24 ankyrin (ANK) repeats of ankyrins bind to numerous membrane proteins, linking them to spectrin-based cytoskeletons at specific membrane microdomains. The accessibility of the target binding groove of ANK repeats must be regulated to achieve spatially defined functions of ankyrins/target complexes in different tissues, though little is known in this regard. Here we systemically investigated the autoinhibition mechanism of ankyrin-B/G by combined biochemical, biophysical and structural biology approaches. We discovered that the entire ANK repeats are inhibited by combinatorial and quasi-independent bindings of multiple disordered segments located in the ankyrin-B/G linkers and tails, suggesting a mechanistic basis for differential regulations of membrane target bindings by ankyrins. In addition to elucidating the autoinhibition mechanisms of ankyrins, our study may also shed light on regulations on target bindings by other long repeat-containing proteins.

Indexed as

AnimalsAnkyrinsCell LineCrystallography, X-RayDogsHumansMiceModels, MolecularProtein ConformationRatsANK2 protein, humanAnk3 protein, ratAnkyrinsAnkyrin-R/B/Gankyrin repeatsautoinhibitionaxon initial segmentbiophysicsnonestructural biology

Identifiers

PMID28841137
PMCPMC5779224
OpenAlexW2747117709

What OpenQuestion holds

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Registered trials

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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.