ArticleCell motility and the cytoskeleton2008
Modulation of actin mechanics by caldesmon and tropomyosin.
Article in Cell motility and the cytoskeleton, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 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
30 citing papers in PubMed, 51 citations in OpenAlex.
- CaMKII generates actin bundle morphology and mechanics distinct from canonical bivalent cross-linkers.bioRxiv : the preprint server for biology · 2026Article
- Sensing the shape of a surface by tightly surface-bound filaments.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Red blood cell-derived materials for cancer therapy: Construction, distribution, and applications.Materials today. Bio · 2024Review
- Twist response of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Alterations of actin cytoskeleton and arterial protein level in patients with obstructive jaundice.Genetics and molecular biology · 2022Article
- Actin filament oxidation by MICAL1 suppresses protections from cofilin-induced disassembly.EMBO reports · 2021Article
- High-speed AFM reveals subsecond dynamics of cardiac thin filaments upon CaProceedings of the National Academy of Sciences of the United States of America · 2019Article
- The Primary Causes of Muscle Dysfunction Associated with the Point Mutations in Tpm3.12; Conformational Analysis of Mutant Proteins as a Tool for Classification of Myopathies.International journal of molecular sciences · 2018Article
- Alternative splicing of the Caenorhabditis elegans lev-11 tropomyosin gene is regulated in a tissue-specific manner.Cytoskeleton (Hoboken, N.J.) · 2018Article
- Atomic insights into the genesis of cellular filaments by globular proteins.Nature structural & molecular biology · 2018Article
- Fungal Morphogenesis, from the Polarized Growth of Hyphae to Complex Reproduction and Infection Structures.Microbiology and molecular biology reviews : MMBR · 2018Review
- The molecular basis of thin filament activation: from single molecule to muscle.Scientific reports · 2017Article
- Stabilizing the central part of tropomyosin increases the bending stiffness of the thin filament.Biophysical journal · 2015Article
- Mechanism of calponin stabilization of cross-linked actin networks.Biophysical journal · 2014Article
- Analysis of flexural rigidity of actin filaments propelled by surface adsorbed myosin motors.Cytoskeleton (Hoboken, N.J.) · 2013Article
- Emergent complexity of the cytoskeleton: from single filaments to tissue.Advances in physics · 2013Review
- Effects of basic calponin on the flexural mechanics and stability of F-actin.Cytoskeleton (Hoboken, N.J.) · 2012Article
- Structural implications of conserved aspartate residues located in tropomyosin's coiled-coil core.Bioarchitecture · 2011Article
- Cofilin-linked changes in actin filament flexibility promote severing.Biophysical journal · 2011Article
- Origin of twist-bend coupling in actin filaments.Biophysical journal · 2010Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
The ability of cells to sense and respond to physiological forces relies on the actin cytoskeleton, a dynamic structure that can directly convert forces into biochemical signals. Because of the association of muscle actin-binding proteins (ABPs) may affect F-actin and hence cytoskeleton mechanics, we investigated the effects of several ABPs on the mechanical properties of the actin filaments. The structural interactions between ABPs and helical actin filaments can vary between interstrand interactions that bridge azimuthally adjacent actin monomers between filament strands (i.e. by molecular stapling as proposed for caldesmon) or, intrastrand interactions that reinforce axially adjacent actin monomers along strands (i.e. as in the interaction of tropomyosin with actin). Here, we analyzed thermally driven fluctuations in actin's shape to measure the flexural rigidity of actin filaments with different ABPs bound. We show that the binding of phalloidin increases the persistence length of actin by 1.9-fold. Similarly, the intrastrand reinforcement by smooth and skeletal muscle tropomyosins increases the persistence length 1.5- and 2- fold respectively. We also show that the interstrand crosslinking by the C-terminal actin-binding fragment of caldesmon, H32K, increases persistence length by 1.6-fold. While still remaining bound to actin, phosphorylation of H32K by ERK abolishes the molecular staple (Foster et al. 2004. J Biol Chem 279;53387-53394) and reduces filament rigidity to that of actin with no ABPs bound. Lastly, we show that the effect of binding both smooth muscle tropomyosin and H32K is not additive. The combination of structural and mechanical studies on ABP-actin interactions will help provide information about the biophysical mechanism of force transduction in cells.
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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.