Evidence map›Paper›PMID 39969983›Full record

ArticleMolecular biology of the cell2025

Calponin-homology domain of GAS2L1 promotes formation of stress fibers and focal adhesions.

Franco K C Au, Khoi T D Le, Zhitao Liao, Zhijie Lin, Yuehong Shen, Penger Tong, Mingjie Zhang, Robert Z Qi

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Molecular biology of the cell, 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.

  1. 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

8 authors.

Franco K C AuDivision of Life Science and State Key Laboratory of Molecular Neuroscience, The Hong Kong University of Science and Technology, Hong Kong, China.
Khoi T D LeDivision of Life Science and State Key Laboratory of Molecular Neuroscience, The Hong Kong University of Science and Technology, Hong Kong, China.
Zhitao LiaoDepartment of Physics, The Hong Kong University of Science and Technology, Hong Kong, China.
Zhijie LinDivision of Life Science and State Key Laboratory of Molecular Neuroscience, The Hong Kong University of Science and Technology, Hong Kong, China.
Yuehong ShenDivision of Life Science and State Key Laboratory of Molecular Neuroscience, The Hong Kong University of Science and Technology, Hong Kong, China.
Penger TongDepartment of Physics, The Hong Kong University of Science and Technology, Hong Kong, China.
Mingjie ZhangDivision of Life Science and State Key Laboratory of Molecular Neuroscience, The Hong Kong University of Science and Technology, Hong Kong, China.
Robert Z QiDivision of Life Science and State Key Laboratory of Molecular Neuroscience, The Hong Kong University of Science and Technology, Hong Kong, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Growth arrest-specific 2-like 1 protein (GAS2L1) binds both actin and microtubules through its unique structural domains: a calponin-homology (CH) domain for actin binding and a GAS2-related (GAR) domain for microtubule interaction. In this study, we demonstrate that GAS2L1 promotes stress fiber assembly, enhances focal adhesion formation, and stabilizes cytoskeletal networks against mechanical perturbation through its CH domain. Remarkably, we show that the CH domain dimerizes and induces actin filament bundling and stabilization both in cells and in vitro. The CH and GAR domains interact to form an autoinhibitory module, wherein the GAR domain suppresses CH domain dimerization and actin-bundling activity. Our findings provide novel insights into the regulatory mechanisms of GAS2L1's autoinhibition and identify the CH domain as a critical actin-bundling factor that contributes to the organization of stress fibers and focal adhesions.

Indexed as

Cell Cycle ProteinsFocal AdhesionsMicrofilament ProteinsStress FibersActin CytoskeletonActinsAnimalsCalcium-Binding ProteinsCalponinsCytoskeletonHumansMicrotubulesProtein BindingProtein DomainsActinsCalcium-Binding ProteinsCalponinsCell Cycle ProteinsMicrofilament Proteins

Identifiers

PMID39969983
PMCPMC12005110

What OpenQuestion holds

Textmetadata
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.