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Published 6 November 2006. doi:10.1083/jcb.200602085
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 175, Number 3, 477-490
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Article

 Reassembly of contractile actin cortex in cell blebs

Guillaume T. Charras1, Chi-Kuo Hu1,2, Margaret Coughlin1, and Timothy J. Mitchison1

1 Department of Systems Biology and 2 Graduate Program in Biological and Biomedical Sciences, Harvard Medical School, Boston, MA 02115

Correspondence to Guillaume Charras: gcharras{at}hms.harvard.edu

Contractile actin cortex is involved in cell morphogenesis, movement, and cytokinesis, but its organization and assembly are poorly understood. During blebbing, the membrane detaches from the cortex and inflates. As expansion ceases, contractile cortex reassembles under the membrane and drives bleb retraction. This cycle enabled us to measure the temporal sequence of protein recruitment to the membrane during cortex reassembly and to explore dependency relationships. Expanding blebs were devoid of actin, but proteins of the erythrocytic submembranous cytoskeleton were present. When expansion ceased, ezrin was recruited to the membrane first, followed by actin, actin-bundling proteins, and, finally, contractile proteins. Complete assembly of the contractile cortex, which was organized into a cagelike mesh of filaments, took ~30 s. Cytochalasin D blocked recruitment of actin and {alpha}-actinin, but had no effect on membrane association of ankyrin B and ezrin. Ezrin played no role in actin nucleation, but was essential for tethering the membrane to the cortex. The Rho pathway was important for cortex assembly in blebs.

Abbreviations used in this paper: ERM, ezrin-radixin-moesin; FERM, four one ERM; GAP, GTPase-activating protein; GDI, guanine nucleotide dissociation inhibitor; GEF, guanine nucleotide exchange factor; MHC, myosin heavy chain; mRFP, monomeric red fluorescent protein; MRLC, myosin regulatory light chain; PH-PLC{delta}, PH domain of phospholipase C {delta}; PIP2, phosphotidylinositol bisphosphate; SEM, scanning electron microscopy; TEM, transmission electron microscopy; TDRFP, tandem dimer RFP.


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