Evidence map›Paper›PMID 35020457›Full record

ArticleMolecular biology of the cell2022

Nanoscale dynamics of actin filaments in the red blood cell membrane skeleton.

Roberta B Nowak, Haleh Alimohamadi, Kersi Pestonjamasp, Padmini Rangamani, Velia M Fowler

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Active Force Dynamics in Red Blood Cells Under Non-Invasive Optical Tweezers.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Dynamic mechanisms for membrane skeleton transitions.bioRxiv : the preprint server for biology · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. 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 1 country.

Roberta B NowakDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037.
Haleh AlimohamadiDepartment of Mechanical and Aerospace Engineering, University of California, San Diego, La Jolla, CA 92093.
Kersi PestonjamaspDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037.
Padmini RangamaniDepartment of Mechanical and Aerospace Engineering, University of California, San Diego, La Jolla, CA 92093.
Velia M FowlerDepartment of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037.
Scripps Research Institute · USUniversity of California San Diego · US

Funding

Capping Actin Growth in Erythroid and Nonerythroid CellsR01HL083464 · NHLBI · UNIVERSITY OF DELAWARE · PI FOWLER, VELIA M · 2006 to 2019
$7.1M
Modeling and analysis of the mechanochemical processes that govern clathrin-mediated endocytosisR01GM132106 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI RANGAMANI, PADMINI · 2020 to 2024
$1.5M
NHLBI NIH HHS R01 HL083464NIGMS NIH HHS R01 GM132106
6 · The paper itself

Abstract

Red blood cell (RBC) shape and deformability are supported by a planar network of short actin filament (F-actin) nodes (∼37 nm length, 15-18 subunits) interconnected by long spectrin strands at the inner surface of the plasma membrane. Spectrin-F-actin network structure underlies quantitative modeling of forces controlling RBC shape, membrane curvature, and deformation, yet the nanoscale organization and dynamics of the F-actin nodes in situ are not well understood. We examined F-actin distribution and dynamics in RBCs using fluorescent-phalloidin labeling of F-actin imaged by multiple microscopy modalities. Total internal reflection fluorescence and Zeiss Airyscan confocal microscopy demonstrate that F-actin is concentrated in multiple brightly stained F-actin foci ∼200-300 nm apart interspersed with dimmer F-actin staining regions. Single molecule stochastic optical reconstruction microscopy imaging of Alexa 647-phalloidin-labeled F-actin and computational analysis also indicates an irregular, nonrandom distribution of F-actin nodes. Treatment of RBCs with latrunculin A and cytochalasin D indicates that F-actin foci distribution depends on actin polymerization, while live cell imaging reveals dynamic local motions of F-actin foci, with lateral movements, appearance and disappearance. Regulation of F-actin node distribution and dynamics via actin assembly/disassembly pathways and/or via local extension and retraction of spectrin strands may provide a new mechanism to control spectrin-F-actin network connectivity, RBC shape, and membrane deformability.

Indexed as

Actin CytoskeletonActinsErythrocyte MembraneErythrocytesSpectrinActinsSpectrin

Identifiers

PMID35020457
PMCPMC9250383
OpenAlexW4205450962

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.