The filopodial myosin DdMyo7 is a slow, calcium-regulated motor.

Casey Eddington, Margaret A Titus

Abstract read

In one paragraph

Article in The Journal of biological chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it

0cells of the map it votes in

1citing 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

1 citing paper in PubMed.

Modulation of Filopodial Myosin Function.bioRxiv : the preprint server for biology · 2025
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

2 authors.

Casey EddingtonDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota, USA; Graduate Program in Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA.

Margaret A TitusDepartment of Genetics, Cell Biology, and Development, University of Minnesota, Minneapolis, Minnesota, USA; Graduate Program in Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, Minnesota, USA. Electronic address: titus004@umn.edu.

Funding

Mechanism of myosin motor-dependent filopodia formationR01GM122917 · NIGMS · UNIVERSITY OF MINNESOTA · PI TITUS, MARGARET A · 2017 to 2024

$3.2M

Characterization of a Filopodial MyosinF31GM139366 · NIGMS · UNIVERSITY OF MINNESOTA · PI EDDINGTON, CASEY W · 2021 to 2022

$64k

NIGMS NIH HHS F31 GM139366NIGMS NIH HHS R01 GM122917

6 · The paper itself

Abstract

MyTH4-FERM (MF) myosins are a family of molecular motors with critical roles in the formation and organization of thin membrane protrusions supported by parallel bundles of actin - filopodia, microvilli, and stereocilia. The amoeboid MF myosin DdMyo7 is essential for filopodia formation but its mechanism of action is unknown. The motor properties of a forced-dimer of the DdMyo7 motor were characterized using an in vitro motility assay to address this question. The DdMyo7 motor associates with two different light chains, the Dictyostelium calmodulins CalA and CalB, whose binding is shown to be sensitive to the presence of calcium. Total internal reflection fluorescence motility assays of the dimerized DdMyo7 motor reveal that it is a slow, processive motor that moves along actin at ∼ 40 nm/sec, and the activity of the motor is significantly reduced in the presence of Ca

Indexed as

CalciumDictyosteliumMyosinsProtozoan ProteinsPseudopodiaActinsAnimalsHumansProtein MultimerizationActinsCalciumMyosinsProtozoan Proteinsactin cytoskeletonDdMyo7filopodiamolecular motorMyTH4-FERM myosinunconventional myosin

Identifiers

PMID40043952

DOI10.1016/j.jbc.2025.108371

PMCPMC12125552

What Socratic holds

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LicenceCC BY

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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 Socratic graph.