ArticleBiology open2013
Requirement of LIM domains for the transient accumulation of paxillin at damaged stress fibres.
Article in Biology open, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed, 16 citations in OpenAlex.
- Tandem LIM domain-containing proteins, LIMK1 and LMO1, directly bind to force-bearing keratin intermediate filaments.Cell reports · 2024Article
- PINCH1 Promotes Fibroblast Migration in Extracellular Matrices and Influences Their Mechanophenotype.Frontiers in cell and developmental biology · 2022Article
- Spatial proximity of proteins surrounding zyxin under force-bearing conditions.Molecular biology of the cell · 2021Article
- LIM domain proteins in cell mechanobiology.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Mechanosensing through Direct Binding of Tensed F-Actin by LIM Domains.Developmental cell · 2020Article
- Mechanosensitive regulation of stanniocalcin-1 by zyxin and actin-myosin in human mesenchymal stromal cells.Stem cells (Dayton, Ohio) · 2020Article
- Roles of paxillin family members in adhesion and ECM degradation coupling at invadosomes.The Journal of cell biology · 2016Article
- Functions of the Tumor Suppressors p53 and Rb in Actin Cytoskeleton Remodeling.BioMed research international · 2016Review
- LIM proteins in actin cytoskeleton mechanoresponse.Trends in cell biology · 2014Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cells recognize and respond to changes in intra- and extracellular mechanical conditions to maintain their mechanical homeostasis. Linear contractile bundles of actin filaments and myosin II known as stress fibres (SFs) mediate mechanical signals. Mechanical cues such as excessive stress driven by myosin II and/or external force may damage SFs and induce the local transient accumulation of SF-repair complexes (zyxin and VASP) at the damaged sites. Using an atomic force microscope mounted on a fluorescence microscope, we applied mechanical damage to cells expressing fluorescently tagged cytoskeletal proteins and recorded the subsequent mobilization of SF-repair complexes. We found that a LIM protein, paxillin, transiently accumulated at the damaged sites earlier than zyxin, while paxillin knockdown did not affect the kinetics of zyxin translocation. The C-terminal half of paxillin, comprising four-tandem LIM domains, can still translocate to damaged sites on SFs, suggesting that the LIM domain is essential for the mechanosensory function of paxillin. Our findings demonstrate a crucial role of the LIM domain in mechanosensing LIM proteins.
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Registered trials
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.