Measuring molecular rupture forces between single actin filaments and actin-binding proteins Export

@article{citeulike:3339759, abstract = {Actin-binding proteins (ABPs) regulate the assembly of actin filaments (F-actin) into networks and bundles that provide the structural integrity of the cell. Two of these ABPs, filamin and α-actinin, have been extensively used to model the mechanical properties of actin networks grown ; however, there is a lack in the understanding of how the molecular interactions between ABPs and F-actin regulate the dynamic properties of the cytoskeleton. Here, we present a native-like assay geometry to test the rupture force of a complex formed by an ABP linking two quasiparallel actin filaments. We readily demonstrate the adaptability of this assay by testing it with two different ABPs: filamin and α-actinin. For filamin/actin and α-actinin/actin, we measured similar rupture forces of 40–80 pN for loading rates between 4 and 50 pN/s. Both ABP unfolding and conformational transition events were observed, demonstrating that both are important and may be a significant mechanism for the temporal regulation of the mechanical properties of the actin cytoskeleton. With this modular, single-molecule assay, a wide range of ABP/actin interactions can be studied to better understand cytoskeletal and cell dynamics.}, author = {Ferrer, Jorge M. and Lee, Hyungsuk and Chen, Jiong and Pelz, Benjamin and Nakamura, Fumihiko and Kamm, Roger D. and Lang, Matthew J.}, citeulike-article-id = {3339759}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0706124105}, citeulike-linkout-1 = {http://www.pnas.org/content/105/27/9221.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/105/27/9221.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/18591676}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=18591676}, doi = {10.1073/pnas.0706124105}, journal = {Proceedings of the National Academy of Sciences}, keywords = {cytoskeletal-dynamics, single-molecule-methods}, month = {July}, number = {27}, pages = {9221--9226}, posted-at = {2009-05-06 10:59:00}, priority = {0}, title = {Measuring molecular rupture forces between single actin filaments and actin-binding proteins}, url = {http://dx.doi.org/10.1073/pnas.0706124105}, volume = {105}, year = {2008} }

TY - JOUR ID - citeulike:3339759 L3 - citeulike-article-id:3339759 N2 - Actin-binding proteins (ABPs) regulate the assembly of actin filaments (F-actin) into networks and bundles that provide the structural integrity of the cell. Two of these ABPs, filamin and α-actinin, have been extensively used to model the mechanical properties of actin networks grown ; however, there is a lack in the understanding of how the molecular interactions between ABPs and F-actin regulate the dynamic properties of the cytoskeleton. Here, we present a native-like assay geometry to test the rupture force of a complex formed by an ABP linking two quasiparallel actin filaments. We readily demonstrate the adaptability of this assay by testing it with two different ABPs: filamin and α-actinin. For filamin/actin and α-actinin/actin, we measured similar rupture forces of 40–80 pN for loading rates between 4 and 50 pN/s. Both ABP unfolding and conformational transition events were observed, demonstrating that both are important and may be a significant mechanism for the temporal regulation of the mechanical properties of the actin cytoskeleton. With this modular, single-molecule assay, a wide range of ABP/actin interactions can be studied to better understand cytoskeletal and cell dynamics. IS - 27 JF - Proceedings of the National Academy of Sciences EP - 9226 TI - Measuring molecular rupture forces between single actin filaments and actin-binding proteins VL - 105 SP - 9221 KW - cytoskeletal-dynamics KW - single-molecule-methods AU - Ferrer, Jorge AU - Lee, Hyungsuk AU - Chen, Jiong AU - Pelz, Benjamin AU - Nakamura, Fumihiko AU - Kamm, Roger AU - Lang, Matthew PY - 2008/07// UR - http://dx.doi.org/10.1073/pnas.0706124105 ER -