ArticleJournal of molecular biology2010
α-actinin is required for the proper assembly of Z-disk/focal-adhesion-like structures and for efficient locomotion in Caenorhabditis elegans.
Article in Journal of molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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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
23 citing papers in PubMed, 33 citations in OpenAlex.
- Linear Z-line-like alignment of capping protein in obliquely striated muscle of the nematodeMolecular biology of the cell · 2026Article
- Linear Z-line-like alignment of capping protein in obliquely striated muscle of the nematodebioRxiv : the preprint server for biology · 2025Article
- FHOD-1 and profilin protect sarcomeres against contraction-induced deformation> inMolecular biology of the cell · 2024Article
- FHOD-1/profilin-mediated actin assembly protects sarcomeres against contraction-induced deformation inbioRxiv : the preprint server for biology · 2024Article
- Disruption of Z-Disc Function Promotes Mechanical Dysfunction in Human Myocardium: Evidence for a Dual Myofilament Modulatory Role by Alpha-Actinin 2.International journal of molecular sciences · 2023Article
- Mono- and Biallelic Protein-Truncating Variants in Alpha-Actinin 2 Cause Cardiomyopathy Through Distinct Mechanisms.Circulation. Genomic and precision medicine · 2021Article
- Investigating the correlation of muscle function tests and sarcomere organization in C. elegans.Skeletal muscle · 2021Article
- FLN-1/filamin is required to anchor the actomyosin cytoskeleton and for global organization of sub-cellular organelles in a contractile tissue.Cytoskeleton (Hoboken, N.J.) · 2020Article
- Kettin, the large actin-binding protein with multiple immunoglobulin domains, is essential for sarcomeric actin assembly and larval development in Caenorhabditis elegans.The FEBS journal · 2020Article
- Tissue-Specific Functions ofG3 (Bethesda, Md.) · 2018Article
- Article
- High-resolution imaging of muscle attachment structures in Caenorhabditis elegans.Cytoskeleton (Hoboken, N.J.) · 2017Article
- Plastin increases cortical connectivity to facilitate robust polarization and timely cytokinesis.The Journal of cell biology · 2017Article
- Molecular evolution of troponin I and a role of its N-terminal extension in nematode locomotion.Cytoskeleton (Hoboken, N.J.) · 2016Article
- The integrin-adhesome is required to maintain muscle structure, mitochondrial ATP production, and movement forces in Caenorhabditis elegans.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2015Article
- The actinin family of actin cross-linking proteins - a genetic perspective.Cell & bioscience · 2015Article
- Regulation of structure and function of sarcomeric actin filaments in striated muscle of the nematode Caenorhabditis elegans.Anatomical record (Hoboken, N.J. : 2007) · 2014Review
- ZYX-1, the unique zyxin protein of Caenorhabditis elegans, is involved in dystrophin-dependent muscle degeneration.Molecular biology of the cell · 2013Article
- α-Actinin2 is required for the lateral alignment of Z discs and ventricular chamber enlargement during zebrafish cardiogenesis.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012Article
- Z-line formins promote contractile lattice growth and maintenance in striated muscles of C. elegans.The Journal of cell biology · 2012Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
The actin binding protein α-actinin is a major component of focal adhesions found in vertebrate cells and of focal-adhesion-like structures found in the body wall muscle of the nematode Caenorhabditis elegans. To study its in vivo function in this genetic model system, we isolated a strain carrying a deletion of the single C. elegans α-actinin gene. We assessed the cytological organization of other C. elegans focal adhesion proteins and the ultrastructure of the mutant. The mutant does not have normal dense bodies, as observed by electron microscopy; however, these dense-body-like structures still contain the focal adhesion proteins integrin, talin, and vinculin, as observed by immunofluorescence microscopy. Actin is found in normal-appearing I-bands, but with abnormal accumulations near muscle cell membranes. Although swimming in water appeared grossly normal, use of automated methods for tracking the locomotion of individual worms revealed a defect in bending. We propose that the reduced motility of α-actinin null is due to abnormal dense bodies that are less able to transmit the forces generated by actin/myosin interactions.
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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.