Dynamic Role of Cross-Linking Proteins in Actin Rheology
We develop a computational model to compare the relative importance of unbinding and unfolding of actin cross-linking proteins (ACPs) in the dynamic properties of the actin cytoskeleton. We show that in the strain-stiffening regime with typical physiological and experimental strain rates, unbinding...
Main Authors: | , , |
---|---|
Other Authors: | |
Format: | Article |
Language: | en_US |
Published: |
Elsevier
2014
|
Online Access: | http://hdl.handle.net/1721.1/92328 https://orcid.org/0000-0002-7232-304X |
_version_ | 1826190623766478848 |
---|---|
author | Kim, Taeyoon Hwang, Wonmuk Kamm, Roger Dale |
author2 | Massachusetts Institute of Technology. Department of Biological Engineering |
author_facet | Massachusetts Institute of Technology. Department of Biological Engineering Kim, Taeyoon Hwang, Wonmuk Kamm, Roger Dale |
author_sort | Kim, Taeyoon |
collection | MIT |
description | We develop a computational model to compare the relative importance of unbinding and unfolding of actin cross-linking proteins (ACPs) in the dynamic properties of the actin cytoskeleton. We show that in the strain-stiffening regime with typical physiological and experimental strain rates, unbinding events are predominant with negligible unfolding. ACPs unbound by greater forces experience larger displacements, with a tendency to rebind to different filaments. At constant strain, stress relaxes to physiological levels by unbinding only—not unfolding—of ACPs, which is consistent with experiments. Also, rebinding of ACPs dampens full relaxation of stress. When the network is allowed to return to a stress-free state after shear deformation, plastic deformation is observed only with unbinding. These results suggest that despite the possibility of unfolding, unbinding of ACPs is the major determinant for the rheology of the actin network. |
first_indexed | 2024-09-23T08:43:11Z |
format | Article |
id | mit-1721.1/92328 |
institution | Massachusetts Institute of Technology |
language | en_US |
last_indexed | 2024-09-23T08:43:11Z |
publishDate | 2014 |
publisher | Elsevier |
record_format | dspace |
spelling | mit-1721.1/923282022-09-23T14:04:32Z Dynamic Role of Cross-Linking Proteins in Actin Rheology Kim, Taeyoon Hwang, Wonmuk Kamm, Roger Dale Massachusetts Institute of Technology. Department of Biological Engineering Massachusetts Institute of Technology. Department of Mechanical Engineering Kamm, Roger Dale We develop a computational model to compare the relative importance of unbinding and unfolding of actin cross-linking proteins (ACPs) in the dynamic properties of the actin cytoskeleton. We show that in the strain-stiffening regime with typical physiological and experimental strain rates, unbinding events are predominant with negligible unfolding. ACPs unbound by greater forces experience larger displacements, with a tendency to rebind to different filaments. At constant strain, stress relaxes to physiological levels by unbinding only—not unfolding—of ACPs, which is consistent with experiments. Also, rebinding of ACPs dampens full relaxation of stress. When the network is allowed to return to a stress-free state after shear deformation, plastic deformation is observed only with unbinding. These results suggest that despite the possibility of unfolding, unbinding of ACPs is the major determinant for the rheology of the actin network. National Institutes of Health (U.S.) (GM076689) 2014-12-16T17:18:24Z 2014-12-16T17:18:24Z 2011-09 2011-03 Article http://purl.org/eprint/type/JournalArticle 00063495 1542-0086 http://hdl.handle.net/1721.1/92328 Kim, Taeyoon, Wonmuk Hwang, and Roger D. Kamm. “Dynamic Role of Cross-Linking Proteins in Actin Rheology.” Biophysical Journal 101, no. 7 (October 2011): 1597–1603. © 2011 Biophysical Society. https://orcid.org/0000-0002-7232-304X en_US http://dx.doi.org/10.1016/j.bpj.2011.08.033 Biophysical Journal Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf Elsevier Elsevier |
spellingShingle | Kim, Taeyoon Hwang, Wonmuk Kamm, Roger Dale Dynamic Role of Cross-Linking Proteins in Actin Rheology |
title | Dynamic Role of Cross-Linking Proteins in Actin Rheology |
title_full | Dynamic Role of Cross-Linking Proteins in Actin Rheology |
title_fullStr | Dynamic Role of Cross-Linking Proteins in Actin Rheology |
title_full_unstemmed | Dynamic Role of Cross-Linking Proteins in Actin Rheology |
title_short | Dynamic Role of Cross-Linking Proteins in Actin Rheology |
title_sort | dynamic role of cross linking proteins in actin rheology |
url | http://hdl.handle.net/1721.1/92328 https://orcid.org/0000-0002-7232-304X |
work_keys_str_mv | AT kimtaeyoon dynamicroleofcrosslinkingproteinsinactinrheology AT hwangwonmuk dynamicroleofcrosslinkingproteinsinactinrheology AT kammrogerdale dynamicroleofcrosslinkingproteinsinactinrheology |