ArticleThe Journal of cell biology2000
Isoforms of alpha-actinin from cardiac, smooth, and skeletal muscle form polar arrays of actin filaments.
Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed.
- 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
- Actin Bundles Dynamics and Architecture.Biomolecules · 2023Review
- Article
- Overexpression of Paxillin Correlates with Tumor Progression and Predicts Poor Survival in Glioblastoma.CNS neuroscience & therapeutics · 2017Article
- Article
- The F-actin bundler α-actinin Ain1 is tailored for ring assembly and constriction during cytokinesis in fission yeast.Molecular biology of the cell · 2016Article
- Electrospun PLGA fibers incorporated with functionalized biomolecules for cardiac tissue engineering.Tissue engineering. Part A · 2014Article
- Three-dimensional architecture of actin filaments in Listeria monocytogenes comet tails.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- Isolation and culture of smooth muscle cells from human acute type A aortic dissection.Journal of cardiothoracic surgery · 2013Article
- The tension mounts: stress fibers as force-generating mechanotransducers.The Journal of cell biology · 2013Review
- In vivo imaging of the actin polymerization state with two-photon fluorescence anisotropy.Biophysical journal · 2012Article
- Actin dynamics associated with focal adhesions.International journal of cell biology · 2012Article
- Actin cross-link assembly and disassembly mechanics for alpha-Actinin and fascin.The Journal of biological chemistry · 2010Article
- Deposition of nonsarcomeric alpha-actinin in cardiomyocytes from patients with dilated cardiomyopathy or chronic pressure overload.Experimental and clinical cardiology · 2009Article
- Novel structures for alpha-actinin:F-actin interactions and their implications for actin-membrane attachment and tension sensing in the cytoskeleton.Journal of molecular biology · 2007Article
- Ca2+ sensitivity of regulated cardiac thin filament sliding does not depend on myosin isoform.The Journal of physiology · 2006Article
- Nanoscale features of fibronectin fibrillogenesis depend on protein-substrate interaction and cytoskeleton structure.Biophysical journal · 2005Article
- An atomic model of actin filaments cross-linked by fimbrin and its implications for bundle assembly and function.The Journal of cell biology · 2001Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
We have used a positively charged lipid monolayer to form two-dimensional bundles of F-actin cross-linked by alpha-actinin to investigate the relative orientation of the actin filaments within them. This method prevents growth of the bundles perpendicular to the monolayer plane, thereby facilitating interpretation of the electron micrographs. Using alpha-actinin isoforms isolated from the three types of vertebrate muscle, i.e., cardiac, skeletal, and smooth, we have observed almost exclusively cross-linking between polar arrays of filaments, i.e., actin filaments with their plus ends oriented in the same direction. One type of bundle can be classified as an Archimedian spiral consisting of a single actin filament that spirals inward as the filament grows and the bundle is formed. These spirals have a consistent hand and grow to a limiting internal diameter of 0.4-0.7 microm, where the filaments appear to break and spiral formation ceases. These results, using isoforms usually characterized as cross-linkers of bipolar actin filament bundles, suggest that alpha-actinin is capable of cross-linking actin filaments in any orientation. Formation of specifically bipolar or polar filament arrays cross-linked by alpha-actinin may require additional factors that either determine the filament orientation or restrict the cross-linking capabilities of alpha-actinin.
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