ArticleMolecular biology of the cell2021
Spatial proximity of proteins surrounding zyxin under force-bearing conditions.
Article in Molecular biology of the cell, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 15 citations in OpenAlex.
- Tandem LIM domain-containing proteins, LIMK1 and LMO1, directly bind to force-bearing keratin intermediate filaments.Cell reports · 2024Article
- Zyxin is important for the stability and function of podocytes, especially during mechanical stretch.Communications biology · 2024Article
- Defined extracellular matrix compositions support stiffness-insensitive cell spreading and adhesion signaling.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Enhancement of Zyxin Promotes Skin Fibrosis by Regulating FAK/PI3K/AKT and TGF-β Signaling Pathways via Integrins.International journal of biological sciences · 2023Article
- TES-1/Tes and ZYX-1/Zyxin protect junctional actin networks under tension during epidermal morphogenesis in the C. elegans embryo.Current biology : CB · 2022Article
- Polo-Like Kinase 2 Plays an Essential Role in Cytoprotection against MG132-Induced Proteasome Inhibition via Phosphorylation of Serine 19 in HSPB5.International journal of molecular sciences · 2022Article
- VASP localization to lipid bilayers induces polymerization driven actin bundle formation.Molecular biology of the cell · 2022Article
- Optical Fluorescence Imaging of Native Proteins Using a Fluorescent Probe with a Cell-Membrane-Permeable Carboxyl Group.International journal of molecular sciences · 2022Article
- Fifteen compelling open questions in plant cell biology.The Plant cell · 2022Review
- Effects of forces on chromatin.APL bioengineering · 2021Review
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
Abstract
Sensing physical forces is a critical first step in mechano-transduction of cells. Zyxin, a LIM domain-containing protein, is recruited to force-bearing actin filaments and is thought to repair and strengthen them. Yet, the precise force-induced protein interactions surrounding zyxin remain unclear. Using BioID analysis, we identified proximal proteins surrounding zyxin under normal and force-bearing conditions by label-free mass spectrometry analysis. Under force-bearing conditions, increased biotinylation of α-actinin 1, α-actinin 4, and AFAP1 were detected, and these proteins accumulated along force-bearing actin fibers independently from zyxin, albeit at a lower intensity than zyxin. VASP also accumulated along force-bearing actin fibers in a zyxin-dependent manner, but the biotinylation of VASP remained constant regardless of force, supporting the model of a free zyxin-VASP complex in the cytoplasm being corecruited to tensed actin fibers. In addition, ARHGAP42, a RhoA GAP, was also identified as a proximal protein of zyxin and colocalized with zyxin along contractile actin bundles. The overexpression of ARHGAP42 reduced the rate of small wound closure, a zyxin-dependent process. These results demonstrate that the application of proximal biotinylation can resolve the proximity and composition of protein complexes as a function of force, which had not been possible with traditional biochemical analysis.
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