ArticleMolecular and cellular biology2014
Human muscle LIM protein dimerizes along the actin cytoskeleton and cross-links actin filaments.
Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 50 citations in OpenAlex.
- Genetics in Hypertrophic Cardiomyopathy: An Evolving Clinical Landscape.Cardiac failure review · 2026Review
- Article
- Exploring Syndecan-4 and MLP and Their Interaction in Primary Cardiomyocytes and H9c2 Cells.Cells · 2024Article
- The actin cytoskeleton in hair bundle development and hearing loss.Hearing research · 2023Review
- Computational analysis of the flexibility in the disordered linker region connecting LIM domains in cysteine-glycine-rich protein.Frontiers in genetics · 2023Article
- Native lamin A/C proteomes and novel partners from heart and skeletal muscle in a mouse chronic inflammation model of human frailty.Frontiers in cell and developmental biology · 2023Article
- Actin cytoskeleton depolymerization increases matrix metalloproteinase gene expression in breast cancer cells by promoting translocation of cysteine-rich protein 2 to the nucleus.Frontiers in cell and developmental biology · 2023Article
- Role of Muscle LIM Protein in Mechanotransduction Process.International journal of molecular sciences · 2022Review
- Muscle LIM Protein Force-Sensing Mediates Sarcomeric Biomechanical Signaling in Human Familial Hypertrophic Cardiomyopathy.Circulation · 2022Article
- Understanding the molecular basis of cardiomyopathy.American journal of physiology. Heart and circulatory physiology · 2022Review
- A mutation in desmin makes skeletal muscle less vulnerable to acute muscle damage after eccentric loading in rats.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- LIM domain proteins in cell mechanobiology.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Skeletal muscle transcriptome in healthy aging.Nature communications · 2021Article
- Coefficient of variation as an image-intensity metric for cytoskeleton bundling.Scientific reports · 2020Article
- Cytoskeletal disorganization underlies PABPN1-mediated myogenic disability.Scientific reports · 2020Article
- Mix and (mis-)match - The mechanosensing machinery in the changing environment of the developing, healthy adult and diseased heart.Biochimica et biophysica acta. Molecular cell research · 2020Review
- Skeletal muscle: A review of molecular structure and function, in health and disease.Wiley interdisciplinary reviews. Systems biology and medicine · 2020Review
- An Overview of the Cytoskeleton-Associated Role of PDLIM5.Frontiers in physiology · 2020Review
- The role of muscle LIM protein in the nervous system.Neural regeneration research · 2019Article
- MLP-deficient human pluripotent stem cell derived cardiomyocytes develop hypertrophic cardiomyopathy and heart failure phenotypes due to abnormal calcium handling.Cell death & disease · 2019Article
Corrections and comments
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Authors and funding
9 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The muscle LIM protein (MLP) is a nucleocytoplasmic shuttling protein playing important roles in the regulation of myocyte remodeling and adaptation to hypertrophic stimuli. Missense mutations in human MLP or its ablation in transgenic mice promotes cardiomyopathy and heart failure. The exact function(s) of MLP in the cytoplasmic compartment and the underlying molecular mechanisms remain largely unknown. Here, we provide evidence that MLP autonomously binds to, stabilizes, and bundles actin filaments (AFs) independently of calcium and pH. Using total internal reflection fluorescence microscopy, we have shown how MLP cross-links actin filaments into both unipolar and mixed-polarity bundles. Quantitative analysis of the actin cytoskeleton configuration confirmed that MLP substantially promotes actin bundling in live myoblasts. In addition, bimolecular fluorescence complementation (BiFC) assays revealed MLP self-association. Remarkably, BiFC complexes mostly localize along actin filament-rich structures, such as stress fibers and sarcomeres, supporting a functional link between MLP self-association and actin cross-linking. Finally, we have demonstrated that MLP self-associates through its N-terminal LIM domain, whereas it binds to AFs through its C-terminal LIM domain. Together our data support that MLP contributes to the maintenance of cardiomyocyte cytoarchitecture by a mechanism involving its self-association and actin filament cross-linking.
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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.