help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH

Biophys. J. BioFAST: First Published November 30, 2007. doi:10.1529/biophysj.107.119743
© 2007 by the Biophysical Society.


A more recent version of this article appeared on April 15, 2008.
This Article
Right arrow Full Text (Rapid PDF)
Right arrow Supplement
Right arrow All Versions of this Article:
biophysj.107.119743v1
94/8/2955    most recent
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow Author home page(s):
Mark Bathe
Claus Heussinger
Mireille M. A. E. Claessens
Andreas Bausch
Erwin Frey
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bathe, M.
Right arrow Articles by Frey, E.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bathe, M.
Right arrow Articles by Frey, E.

BIOPHYSICAL THEORY AND MODELING

Cytoskeletal bundle mechanics

Mark Bathe 1, Claus Heussinger 1, Mireille M. A. E. Claessens 2, Andreas Bausch 2 and Erwin Frey 1*

1 Ludwig-Maximilians-Universitaet Muenchen
2 Technische Universitaet Muenchen

* To whom correspondence should be addressed. E-mail: frey{at}lmu.de.

Submitted on August 21, 2007
Revised on September 23, 2007
Accepted on 6 November 2007


   Abstract
The mechanical properties of cytoskeletal actin bundles play an essential role in numerous physiological processes including hearing, fertilization, cell migration and growth. Cells employ a multitude of actin-binding proteins to regulate actively bundle dimensions and crosslinking properties to suit biological function. The mechanical properties of actin bundles vary by orders of magnitude depending on diameter and length, crosslinking protein type and concentration, and constituent filament properties. Despite their importance to cell function, the molecular design principles responsible for this mechanical behavior remain unknown. Here, we examine the mechanics of cytoskeletal bundles using a molecular-based model that accounts for the discrete nature of constituent actin filaments and their distinct crosslinking proteins. A generic competition between filament stretching and crosslink shearing determines three markedly different regimes of mechanical response that are delineated by the relative values of two simple design parameters, revealing the universal nature of bundle bending mechanics. In each regime, bundle bending stiffness displays distinct scaling behavior with respect to bundle dimensions and molecular composition, as observed in reconstituted actin bundles in vitro. This mechanical behavior has direct implications on the physiological bending, buckling, and entropic stretching behavior of cytoskeletal processes, as well as reconstituted actin systems. Results are used to predict the bending regime of various in vivo cytoskeletal bundles that are not easily accessible to experiment and to generate hypotheses regarding implications of the isolated behavior on in vivo bundle function.

Key Words: actin, fascin, filopodium, fimbrin, stereocilium




This article has been cited by other articles:


Home page
Proc. Natl. Acad. Sci. USAHome page
M. M. A. E. Claessens, C. Semmrich, L. Ramos, and A. R. Bausch
Helical twist controls the thickness of F-actin bundles
PNAS, July 1, 2008; 105(26): 8819 - 8822.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
Copyright © 2007 by the Biophysical Society.