ArticleBiophysical journal2008
Molecular mechanics of filamin's rod domain.
Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 36 citations in OpenAlex.
- Quantitative proteomics reveals FLNC as a potential progression marker for the development of hepatocellular carcinoma.Oncotarget · 2016Article
- Multiscale mechanobiology: computational models for integrating molecules to multicellular systems.Integrative biology : quantitative biosciences from nano to macro · 2015Review
- New cancer suppressor gene for colorectal adenocarcinoma: filamin A.World journal of gastroenterology · 2015Article
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- The interaction of vinculin with actin.PLoS computational biology · 2013Article
- A molecular trajectory of α-actinin activation.Biophysical journal · 2012Article
- Filamins in mechanosensing and signaling.Annual review of biophysics · 2012Review
- Filamin structure, function and mechanics: are altered filamin-mediated force responses associated with human disease?Biophysical reviews · 2011Review
- A molecular dynamics investigation of vinculin activation.Biophysical journal · 2010Article
- Molecular Biomechanics: The Molecular Basis of How Forces Regulate Cellular Function.Molecular & cellular biomechanics : MCB · 2010Article
- Phosphorylation facilitates the integrin binding of filamin under force.Biophysical journal · 2009Article
- Conformational changes and signaling in cell and matrix physics.Current biology : CB · 2009Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rearrangement of the actin cytoskeleton is integral to cell shape and function. Actin-binding proteins, e.g., filamin, can naturally contribute to the mechanics and function of the actin cytoskeleton. The molecular mechanical bases for filamin's function in actin cytoskeletal reorganization are examined here using molecular dynamics simulations. Simulations are performed by applying forces ranging from 25 pN to 125 pN for 2.5 ns to the rod domain of filamin. Applying small loads ( approximately 25 pN) to filamin's rod domain supplies sufficient energy to alter the conformation of the N-terminal regions of the rod. These forces break local hydrogen bond coordination often enough to allow side chains to find new coordination partners, in turn leading to drastic changes in the conformation of filamin, for example, increasing the hydrophobic character of the N-terminal rod region and, alternatively, activating the C-terminal region to become increasingly stiff. These changes in conformation can lead to changes in the affinity of filamin for its binding partners. Therefore, filamin can function to transduce mechanical signals as well as preserve topology of the actin cytoskeleton throughout the rod domain.
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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.