β- and γ-cytoplasmic actins display distinct distribution and functional diversity
Open Access
- 15 August 2009
- journal article
- Published by The Company of Biologists in Journal of Cell Science
- Vol. 122 (16), 2980-2988
- https://doi.org/10.1242/jcs.041970
Abstract
Using newly generated monoclonal antibodies, we have compared the distribution of β- and γ-cytoplasmic actin in fibroblastic and epithelial cells, in which they play crucial roles during various key cellular processes. Whereas β-actin is preferentially localized in stress fibers, circular bundles and at cell-cell contacts, suggesting a role in cell attachment and contraction, γ-actin displays a more versatile organization, according to cell activities. In moving cells, γ-actin is mainly organized as a meshwork in cortical and lamellipodial structures, suggesting a role in cell motility; in stationary cells, γ-actin is also recruited into stress fibers. β-actin-depleted cells become highly spread, display broad protrusions and reduce their stress-fiber content; by contrast, γ-actin-depleted cells acquire a contractile phenotype with thick actin bundles and shrinked lamellar and lamellipodial structures. Moreover, β- and γ-actin depleted fibroblasts exhibit distinct changes in motility compared with their controls, suggesting a specific role for each isoform in cell locomotion. Our results reveal new aspects of β- and γ-actin organization that support their functional diversity.Keywords
This publication has 60 references indexed in Scilit:
- Nonmuscle myosin II is responsible for maintaining endothelial cell basal tone and stress fiber integrityAmerican Journal of Physiology-Cell Physiology, 2008
- WASP family members and formin proteins coordinate regulation of cell protrusions in carcinoma cellsThe Journal of cell biology, 2008
- The many faces of actin: matching assembly factors with cellular structuresNature Cell Biology, 2007
- Mechanism of Blebbistatin Inhibition of Myosin IIJournal of Biological Chemistry, 2004
- Cell Migration: Integrating Signals from Front to BackScience, 2003
- Arp2/3 Complex and Actin Depolymerizing Factor/Cofilin in Dendritic Organization and Treadmilling of Actin Filament Array in LamellipodiaThe Journal of cell biology, 1999
- The specific NH2-terminal sequence Ac-EEED of alpha-smooth muscle actin plays a role in polymerization in vitro and in vivo.The Journal of cell biology, 1995
- At least six different actins are expressed in a higher mammal: An analysis based on the amino acid sequence of the amino-terminal tryptic peptideJournal of Molecular Biology, 1978
- Actin content and organization in normal and transformed cells in culture.The Journal of cell biology, 1978
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970