Evidence map›Paper›PMID 33888395›Full record

ReviewTrends in cell biology2021

The state of F-BAR domains as membrane-bound oligomeric platforms.

Chloe E Snider, Wan Nurul Izzati Wan Mohamad Noor, Nhung Thi Hong Nguyen, Kathleen L Gould, Shiro Suetsugu

Abstract readReview
In one paragraph

Review in Trends in cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing 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

12 citing papers in PubMed.

  1. Review
  2. Article
  3. F-BAR Proteins CIP4 and FBP17 Function in Cortical Neuron Radial Migration and Process Outgrowth.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. 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.

Chloe E SniderDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37232, USA.
Wan Nurul Izzati Wan Mohamad NoorDivision of Biological Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
Nhung Thi Hong NguyenDivision of Biological Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan.
Kathleen L GouldDepartment of Cell and Developmental Biology, Vanderbilt University, Nashville, TN 37232, USA. Electronic address: kathy.gould@vanderbilt.edu.
Shiro SuetsuguDivision of Biological Science, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan; Data Science Center, Nara Institute of Science and Technology, 8916-5 Takayama, Ikoma, Nara 630-0192, Japan. Electronic address: suetsugu@bs.naist.jp.

Funding

TRAINING PROGRAM IN CELLULAR, BIOCHEMICAL, &MOLECULAR ST32GM008554 · NIGMS · VANDERBILT UNIVERSITY · PI PATTON, JAMES G. · 1995 to 2020
$7.4M
Regulation of cytokinesisR35GM131799 · NIGMS · VANDERBILT UNIVERSITY · PI Kathleen L Gould · 2019 to 2026
$6.4M
NIGMS NIH HHS R35 GM131799NIGMS NIH HHS T32 GM008554
6 · The paper itself

Abstract

Fes/Cip4 homology Bin/amphiphysin/Rvs (F-BAR) domains, like all BAR domains, are dimeric units that oligomerize and bind membranes. F-BAR domains are generally coupled to additional domains that function in protein binding or have enzymatic activity. Because of their crescent shape and ability to oligomerize, F-BAR domains have been traditionally viewed as membrane-deformation modules. However, multiple independent studies have provided no evidence that certain F-BAR domains are able to tubulate membrane. Instead, a growing body of literature featuring structural, biochemical, biophysical, and microscopy-based studies supports the idea that the F-BAR domain family can be unified only by their ability to form oligomeric assemblies on membranes to provide platforms for molecular assembly.

Indexed as

Cell MembraneHumansMembranesProtein Bindingactin cytoskeletonBAR domainelectron microscopy (EM)F-BAR domainmembrane-bound platformsmembrane linkersoligomeric assembliessuper-resolution microscopy

Identifiers

PMID33888395
PMCPMC8286294

What OpenQuestion holds

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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.