Molecular mechanics of filamin's rod domain. Export

@article{citeulike:2984714, 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.}, address = {Molecular Cell Biomechanics Laboratory, Department of Bioengineering and Biophysics Graduate Group, University of California, Berkeley, California 94720, USA.}, author = {Kolahi, K. S. and Mofrad, M. R.}, citeulike-article-id = {2984714}, citeulike-linkout-0 = {http://dx.doi.org/10.1529/biophysj.107.118802}, citeulike-linkout-1 = {http://linkinghub.elsevier.com/retrieve/pii/S0006349508707033}, citeulike-linkout-2 = {http://view.ncbi.nlm.nih.gov/pubmed/17921200}, citeulike-linkout-3 = {http://www.hubmed.org/display.cgi?uids=17921200}, day = {1}, doi = {10.1529/biophysj.107.118802}, issn = {1542-0086}, journal = {Biophysical journal}, keywords = {force-probe-md, mechanotransduction}, month = {February}, number = {3}, pages = {1075--1083}, posted-at = {2008-07-10 12:47:19}, priority = {4}, title = {Molecular mechanics of filamin's rod domain.}, url = {http://dx.doi.org/10.1529/biophysj.107.118802}, volume = {94}, year = {2008} }

TY - JOUR ID - citeulike:2984714 L3 - citeulike-article-id:2984714 N2 - 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. IS - 3 JF - Biophysical journal SN - 1542-0086 AD - Molecular Cell Biomechanics Laboratory, Department of Bioengineering and Biophysics Graduate Group, University of California, Berkeley, California 94720, USA. EP - 1083 TI - Molecular mechanics of filamin's rod domain. VL - 94 SP - 1075 KW - force-probe-md KW - mechanotransduction AU - Kolahi, KS AU - Mofrad, MR PY - 2008/02/01/ UR - http://dx.doi.org/10.1529/biophysj.107.118802 ER -