Relating Microstructure to Rheology of a Bundled and Cross-Linked F-Actin Network in vitro
The organization of individual actin filaments into higher-order structures is controlled by actin-binding proteins (ABPs). Although the biological significance of the ABPs is well documented, little is known about how bundling and cross-linking quantitatively affect the microstructure and mechanica...
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Veröffentlicht in: | Proceedings of the National Academy of Sciences - PNAS 2004-06, Vol.101 (26), p.9636-9641 |
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creator | Shin, J. H. Gardel, M. L. Mahadevan, L. Matsudaira, P. Weitz, D. A. Lubensky, Tom C. |
description | The organization of individual actin filaments into higher-order structures is controlled by actin-binding proteins (ABPs). Although the biological significance of the ABPs is well documented, little is known about how bundling and cross-linking quantitatively affect the microstructure and mechanical properties of actin networks. Here we quantify the effect of the ABP scruin on actin networks by using imaging techniques, cosedimentation assays, multiparticle tracking, and bulk rheology. We show how the structure of the actin network is modified as the scruin concentration is varied, and we correlate these structural changes to variations in the resultant network elasticity. |
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H. ; Gardel, M. L. ; Mahadevan, L. ; Matsudaira, P. ; Weitz, D. A. ; Lubensky, Tom C.</creator><creatorcontrib>Shin, J. H. ; Gardel, M. L. ; Mahadevan, L. ; Matsudaira, P. ; Weitz, D. A. ; Lubensky, Tom C.</creatorcontrib><description>The organization of individual actin filaments into higher-order structures is controlled by actin-binding proteins (ABPs). Although the biological significance of the ABPs is well documented, little is known about how bundling and cross-linking quantitatively affect the microstructure and mechanical properties of actin networks. Here we quantify the effect of the ABP scruin on actin networks by using imaging techniques, cosedimentation assays, multiparticle tracking, and bulk rheology. We show how the structure of the actin network is modified as the scruin concentration is varied, and we correlate these structural changes to variations in the resultant network elasticity.</description><identifier>ISSN: 0027-8424</identifier><identifier>EISSN: 1091-6490</identifier><identifier>DOI: 10.1073/pnas.0308733101</identifier><identifier>PMID: 15210969</identifier><language>eng</language><publisher>United States: National Academy of Sciences</publisher><subject>Actin Cytoskeleton - chemistry ; Actin Cytoskeleton - metabolism ; Actins ; Actins - chemistry ; Actins - metabolism ; Animals ; Biological Sciences ; Biophysics ; Bundling ; Elasticity ; Gels ; Horseshoe Crabs ; Imaging ; Male ; Mechanical properties ; Microfilaments ; Microscopy, Confocal ; Moduli of elasticity ; Particle motion ; Protein Structure, Quaternary ; Rheology ; Scientific imaging ; Spermatozoa</subject><ispartof>Proceedings of the National Academy of Sciences - PNAS, 2004-06, Vol.101 (26), p.9636-9641</ispartof><rights>Copyright 1993/2004 The National Academy of Sciences of the United States of America</rights><rights>Copyright National Academy of Sciences Jun 29, 2004</rights><rights>Copyright © 2004, The National Academy of Sciences 2004</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c452t-8a976255e36033c51e0be4766232c3a616f107481751b7ca4f0639be6d69833a3</citedby><cites>FETCH-LOGICAL-c452t-8a976255e36033c51e0be4766232c3a616f107481751b7ca4f0639be6d69833a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://www.pnas.org/content/101/26.cover.gif</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/3372509$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/3372509$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,727,780,784,803,885,27924,27925,53791,53793,58017,58250</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/15210969$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Shin, J. H.</creatorcontrib><creatorcontrib>Gardel, M. L.</creatorcontrib><creatorcontrib>Mahadevan, L.</creatorcontrib><creatorcontrib>Matsudaira, P.</creatorcontrib><creatorcontrib>Weitz, D. A.</creatorcontrib><creatorcontrib>Lubensky, Tom C.</creatorcontrib><title>Relating Microstructure to Rheology of a Bundled and Cross-Linked F-Actin Network in vitro</title><title>Proceedings of the National Academy of Sciences - PNAS</title><addtitle>Proc Natl Acad Sci U S A</addtitle><description>The organization of individual actin filaments into higher-order structures is controlled by actin-binding proteins (ABPs). Although the biological significance of the ABPs is well documented, little is known about how bundling and cross-linking quantitatively affect the microstructure and mechanical properties of actin networks. Here we quantify the effect of the ABP scruin on actin networks by using imaging techniques, cosedimentation assays, multiparticle tracking, and bulk rheology. We show how the structure of the actin network is modified as the scruin concentration is varied, and we correlate these structural changes to variations in the resultant network elasticity.</description><subject>Actin Cytoskeleton - chemistry</subject><subject>Actin Cytoskeleton - metabolism</subject><subject>Actins</subject><subject>Actins - chemistry</subject><subject>Actins - metabolism</subject><subject>Animals</subject><subject>Biological Sciences</subject><subject>Biophysics</subject><subject>Bundling</subject><subject>Elasticity</subject><subject>Gels</subject><subject>Horseshoe Crabs</subject><subject>Imaging</subject><subject>Male</subject><subject>Mechanical properties</subject><subject>Microfilaments</subject><subject>Microscopy, Confocal</subject><subject>Moduli of elasticity</subject><subject>Particle motion</subject><subject>Protein Structure, Quaternary</subject><subject>Rheology</subject><subject>Scientific imaging</subject><subject>Spermatozoa</subject><issn>0027-8424</issn><issn>1091-6490</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp90UFvFCEUAGBiNHatnr0YJR5ML9M-YIDh4KFubDVZNWn04oWwDLOdLTuswFT772Wym656kAsEvvfyHg-h5wROCUh2th1MOgUGjWSMAHmAZgQUqUSt4CGaAVBZNTWtj9CTlNYAoHgDj9ER4bQ4oWbo-5XzJvfDCn_qbQwpx9HmMTqcA766dsGH1R0OHTb43Ti03rXYDC2eF5mqRT_clIuL6tyWDPizyz9DvMHleNvnGJ6iR53xyT3b78fo28X7r_MP1eLL5cf5-aKyNae5aoySgnLumADGLCcOlq6WQlBGLTOCiK60WjdEcrKU1tQdCKaWTrRCNYwZdoze7vJux-XGtdYNORqvt7HfmHing-n13y9Df61X4VbXEiSVJf7NPj6GH6NLWW_6ZJ33ZnBhTFqUJXkzwdf_wHUY41B60xQIbYDTpqCzHZp-M0XX3RdCQE8z09PM9GFmJeLln_Uf_H5IBZzswRR5SEc0FVoJJnQ3ep_dr1zoq__TIl7sxDrlEO8JY5JyUOw3DGKzQQ</recordid><startdate>20040629</startdate><enddate>20040629</enddate><creator>Shin, J. 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subjects | Actin Cytoskeleton - chemistry Actin Cytoskeleton - metabolism Actins Actins - chemistry Actins - metabolism Animals Biological Sciences Biophysics Bundling Elasticity Gels Horseshoe Crabs Imaging Male Mechanical properties Microfilaments Microscopy, Confocal Moduli of elasticity Particle motion Protein Structure, Quaternary Rheology Scientific imaging Spermatozoa |
title | Relating Microstructure to Rheology of a Bundled and Cross-Linked F-Actin Network in vitro |
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