Evidence map›Paper›PMID 25717184›Full record

ArticleMolecular biology of the cell2015

Dynamic actin filaments control the mechanical behavior of the human red blood cell membrane.

David S Gokhin, Roberta B Nowak, Joseph A Khoory, Alfonso de la Piedra, Ionita C Ghiran, Velia M Fowler

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.1field-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

32 citing papers in PubMed, 67 citations in OpenAlex.

  1. Article
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  3. ATP-dependent actin barbed-end fluctuations at steady state.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  18. Axonal cytomechanics in neuronal development.Journal of biosciences · 2020
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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 2 institutions in 1 country.

David S GokhinDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037.
Roberta B NowakDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037.
Joseph A KhooryDepartment of Medicine, Beth Israel Deaconess Medical Center, Boston, MA 02115.
Alfonso de la PiedraDepartment of Medicine, Beth Israel Deaconess Medical Center, Boston, MA 02115.
Ionita C GhiranDepartment of Medicine, Beth Israel Deaconess Medical Center, Boston, MA 02115.
Velia M FowlerDepartment of Cell and Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037 velia@scripps.edu.
Beth Israel Deaconess Medical Center · USScripps Research Institute · US

Funding

Capping Actin Growth in Erythroid and Nonerythroid CellsR01HL083464 · NHLBI · UNIVERSITY OF DELAWARE · PI FOWLER, VELIA M · 2006 to 2019
$7.1M
Modulation of erythrocyte function by complementR01HL096795 · NHLBI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI GHIRAN, IONITA CALIN · 2011 to 2014
$1.7M
Structure and Remodeling of the Distal Segment of the Thin FilamentK99AR066534 · NIAMS · SCRIPPS RESEARCH INSTITUTE, THE · PI GOKHIN, DAVID SAMUEL · 2014 to 2015
$178k
NHLBI NIH HHS R01 HL083464NHLBI NIH HHS R01-HL083464NHLBI NIH HHS R01 HL096795NHLBI NIH HHS R01-HL096795NIAMS NIH HHS K99 AR066534
6 · The paper itself

Abstract

Short, uniform-length actin filaments function as structural nodes in the spectrin-actin membrane skeleton to optimize the biomechanical properties of red blood cells (RBCs). Despite the widespread assumption that RBC actin filaments are not dynamic (i.e., do not exchange subunits with G-actin in the cytosol), this assumption has never been rigorously tested. Here we show that a subpopulation of human RBC actin filaments is indeed dynamic, based on rhodamine-actin incorporation into filaments in resealed ghosts and fluorescence recovery after photobleaching (FRAP) analysis of actin filament mobility in intact RBCs (~25-30% of total filaments). Cytochalasin-D inhibition of barbed-end exchange reduces rhodamine-actin incorporation and partially attenuates FRAP recovery, indicating functional interaction between actin subunit turnover at the single-filament level and mobility at the membrane-skeleton level. Moreover, perturbation of RBC actin filament assembly/disassembly with latrunculin-A or jasplakinolide induces an approximately twofold increase or ~60% decrease, respectively, in soluble actin, resulting in altered membrane deformability, as determined by alterations in RBC transit time in a microfluidic channel assay, as well as by abnormalities in spontaneous membrane oscillations (flickering). These experiments identify a heretofore-unrecognized but functionally important subpopulation of RBC actin filaments, whose properties and architecture directly control the biomechanical properties of the RBC membrane.

Indexed as

Actin CytoskeletonActinsBiomechanical PhenomenaCell MembraneErythrocytesHumansOsmotic FragilityProtein MultimerizationActins

Identifiers

PMID25717184
PMCPMC4436781
OpenAlexW2151165459

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.