Evidence map›Paper›PMID 32444496›Full record

ArticleThe Journal of biological chemistry2020

The BAR domain of the Arf GTPase-activating protein ASAP1 directly binds actin filaments.

Pei-Wen Chen, Neil Billington, Ben Y Maron, Jeffrey A Sload, Krishna Chinthalapudi, Sarah M Heissler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

16 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  7. The Janus-faced functions of Apolipoproteins L in membrane dynamics.Cellular and molecular life sciences : CMLS · 2024
    Article
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  14. Bio-protocol · 2022
    Article
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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 3 institutions in 1 country.

Pei-Wen ChenDepartment of Biology, Williams College, Williamstown, Massachusetts, USA.
Neil BillingtonLaboratory of Molecular Physiology, National Heart, Lung, and Blood Institute, Bethesda, Maryland, USA.ORCID 0000-0003-2306-0228
Ben Y MaronDepartment of Biology, Williams College, Williamstown, Massachusetts, USA.
Jeffrey A SloadDepartment of Biology, Williams College, Williamstown, Massachusetts, USA.
Krishna ChinthalapudiDepartment of Physiology and Cell Biology, Dorothy M. Davis Heart and Lung Research Institute, The Ohio State University Wexner Medical Center, Columbus, Ohio, USA.ORCID 0000-0003-3669-561X
Sarah M HeisslerDepartment of Physiology and Cell Biology, Dorothy M. Davis Heart and Lung Research Institute, The Ohio State University Wexner Medical Center, Columbus, Ohio, USA sarah.heissler@osumc.edu.ORCID 0000-0002-6972-7940
Williams College · USThe Ohio State University Wexner Medical Center · USNational Heart Lung and Blood Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Arf GTPase-activating protein (Arf GAP) with SH3 domain, ankyrin repeat and PH domain 1 (ASAP1) establishes a connection between the cell membrane and the cortical actin cytoskeleton. The formation, maintenance, and turnover of actin filaments and bundles in the actin cortex are important for cell adhesion, invasion, and migration. Here, using actin cosedimentation, polymerization, and depolymerization assays, along with total internal reflection fluorescence (TIRF), confocal, and EM analyses, we show that the N-terminal N-BAR domain of ASAP1 directly binds to F-actin. We found that ASAP1 homodimerization aligns F-actin in predominantly unipolar bundles and stabilizes them against depolymerization. Furthermore, the ASAP1 N-BAR domain moderately reduced the spontaneous polymerization of G-actin. The overexpression of the ASAP1 BAR-PH tandem domain in fibroblasts induced the formation of actin-filled projections more effectively than did full-length ASAP1. An ASAP1 construct that lacked the N-BAR domain failed to induce cellular projections. Our results suggest that ASAP1 regulates the dynamics and the formation of higher-order actin structures, possibly through direct binding to F-actin via its N-BAR domain. We propose that ASAP1 is a hub protein for dynamic protein-protein interactions in mechanosensitive structures, such as focal adhesions, invadopodia, and podosomes, that are directly implicated in oncogenic events. The effect of ASAP1 on actin dynamics puts a spotlight on its function as a central signaling molecule that regulates the dynamics of the actin cytoskeleton by transmitting signals from the plasma membrane.

Indexed as

Actin CytoskeletonAdaptor Proteins, Signal TransducingAnimalsMiceNIH 3T3 CellsProtein BindingSignal TransductionAdaptor Proteins, Signal TransducingAsap1 protein, mouseactinactin-binding proteinArf GAP with SH3 domain ankyrin repeat and PH domain 1 (ASAP1)circular dorsal rufflescytoskeletonenzyme mechanismfocal adhesioninvadopodiamechanosensingmembrane dynamicsN-BAR domainprotein complexprotein–protein interaction

Identifiers

PMID32444496
PMCPMC7415992
OpenAlexW3027733014

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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 OpenQuestion graph.