Evidence map›Paper›PMID 39992031›Full record

ArticleCytoskeleton (Hoboken, N.J.)2025

Actin Filament Pointed Ends: Assays for Regulation of Assembly and Disassembly by Tropomodulin and Tropomyosin.

Sawako Yamashiro, Shashank Shekhar, Stefanie M Novak, Sudipta Biswas, Carol C Gregorio, Velia M Fowler

Abstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing 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

4 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. 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

6 authors.

Sawako YamashiroLaboratory of Single-Molecule Cell Biology, Kyoto University Graduate School of Biostudies, Kyoto, Japan.
Shashank ShekharDepartments of Physics, Cell Biology and Biochemistry, Emory University, Atlanta, Georgia, USA.
Stefanie M NovakDepartment of Cellular and Molecular Medicine and Sarver Molecular Cardiovascular Research Program, The University of Arizona, Tucson, Arizona, USA.
Sudipta BiswasDepartments of Physics, Cell Biology and Biochemistry, Emory University, Atlanta, Georgia, USA.
Carol C GregorioDepartment of Cellular and Molecular Medicine and Sarver Molecular Cardiovascular Research Program, The University of Arizona, Tucson, Arizona, USA.
Velia M FowlerDepartment of Biological Sciences, University of Delaware, Newark, Delaware, USA.ORCID https://orcid.org/0000-0002-3161-8802

Funding

Capping Actin Growth in Erythroid and Nonerythroid CellsR01HL083464 · NHLBI · UNIVERSITY OF DELAWARE · PI FOWLER, VELIA M · 2006 to 2019
$7.1M
Membrane Skeleton Regulation of Cell Shape and Interactions in Lens DevelopmentR01EY017724 · NEI · UNIVERSITY OF DELAWARE · PI FOWLER, VELIA M · 2008 to 2024
$6.9M
Deciphering the role of Lmod2 in thin filament length regulation and dilated cardiomyopathyR01HL123078 · NHLBI · UNIVERSITY OF ARIZONA · PI Carol C Gregorio, Shashank Shekhar · 2015 to 2026
$5.6M
REGULATION OF THE ACTIN FILAMENT POINTED END DYNAMICS IN HEALTH AND DISEASER01GM120137 · NIGMS · WASHINGTON STATE UNIVERSITY · PI GALKIN, VITOLD, GREGORIO, CAROL C · 2017 to 2024
$4.0M
MULTICOMPONENT MECHANOCHEMICAL REGULATION OF ACTIN FILAMENT END DYNAMICSR35GM143050 · NIGMS · EMORY UNIVERSITY · PI Shashank Shekhar · 2021 to 2026
$2.7M
Regulation of thin filament architecture by CAP2 in health and myopathyR01HL173431 · NHLBI · ICAHN SCHOOL OF MEDICINE AT MOUNT SINAI · PI Carol C Gregorio · 2025 to 2026
$1.4M
Japan Society for the Promotion of Science KAKENHI JP23H04310Japan Society for the Promotion of Science KAKENHI JP24H01944NEI NIH HHS R01 EY017724NHLBI NIH HHS R01 HL083464NHLBI NIH HHS R01 HL123078NHLBI NIH HHS R01 HL173431NIGMS NIH HHS R01 GM120137NIGMS NIH HHS R35 GM143050NIH HHS R01EY017724NIH HHS R01GM120137NIH HHS R01HL083464NIH HHS R01HL123078NIH HHS R35GM143050
6 · The paper itself

Abstract

Actin filaments are dynamic polymers whose length depends on regulated monomer association and dissociation at their ends. Actin barbed-end dynamics are relatively better understood, primarily due to the approximately tenfold faster subunit on/off rates at barbed versus pointed ends. We present experimental approaches to selectively assay actin pointed-end regulation using bulk biochemistry, single filament imaging, and live cell microscopy with an emphasis on tropomodulins (Tmods), a conserved family of eukaryotic proteins that specifically cap pointed ends. Average pointed-end assembly/disassembly rates are measured in bulk solution using pyrene-labeled actin and barbed end-capping protein CapZ. Direct rate measurements of individual pointed ends are performed via microfluidic-assisted total internal reflection fluorescence microscopy (mf-TIRF). Actin pointed-end dynamics in living cells are examined in striated muscle cells expressing fluorescent actin, where the regular arrays of 1- to 2-μm-long actin filaments in sarcomeres enable visualization of filament pointed and barbed ends. These assays will also help advance our understanding of other pointed end regulators, including cyclase-associated protein and leiomodins, which have been implicated in filament stabilization, disassembly, and elongation. This work is relevant to the musculoskeletal field, where precise regulation of filament lengths is particularly critical for sarcomere organization and striated muscle contraction.

Indexed as

Actin CytoskeletonTropomodulinTropomyosinActinsAnimalsHumansActinsTropomodulinTropomyosinactin polymerizationleiomodinstriated muscle sarcomerestropomodulintropomyosin

Identifiers

PMID39992031
PMCPMC12353072

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.