Separate but not equal: Differential mechanical roles for myosin isoforms

Loading...
Thumbnail Image
Penn collection
Departmental Papers (BE)
Degree type
Discipline
Subject
Funder
Grant number
License
Copyright date
Distributor
Related resources
Contributor
Abstract

Cells undergo many structural-mechanical changes as an inextricable component of cellular motility, cytokinesis, and changes in cell shape. The mere act of receptor-mediated adhesion to extracellular matrix involves massive changes in cytoskeletal organization, spreading, and flattening of cells against the matrix, and the generation of traction forces through the contractile activity of cells. The primary force-generating proteins involved in these mechanical processes are thought to be the nonmuscle myosin II's (NMM-II). Of the three different nonmuscle myosin II isoforms that have been identified, two (NMM-IIA and NMM-IIB) are found almost ubiquitously in higher organisms. Yet, it has remained unclear whether these molecules play redundant, overlapping, or distinct roles in the varying mechanical functions of cells.

Advisor
Date Range for Data Collection (Start Date)
Date Range for Data Collection (End Date)
Digital Object Identifier
Series name and number
Publication date
2007-05-01
Journal title
Volume number
Issue number
Publisher
Publisher DOI
Journal Issue
Comments
Postprint version. Published in Biophysical Journal, Volume 92, Issue 9, May 2007, pages 2984-2985. Publisher URL: http://dx.doi.org/10.1529/biophysj.106.100065
Recommended citation
Collection