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J Muscle Res Cell Motil. 1996 Apr;17(2):269-74.

Myosin-based cortical tension in Dictyostelium resolved into heavy and light chain-regulated components.

Author information

1
Department of Physiology and Biophysics, Case Western Reserve School of Medicine, Cleveland, OH 44106-4970, USA.

Abstract

Cortical tension in most nonmuscle cells is due largely to force production by conventional myosin (myosin II) assembled into the cytoskeleton. Cytoskeletal contraction in smooth muscle and nonmuscle cells is influenced by the degree of myosin filament assembly, and by activation of myosin motor function via regulatory light chain phosphorylation. Recombinant Dictyostelium discoideum cell lines have been generated bearing altered myosin heavy chains, resulting in either constitutive motor function or constitutive assembly into the cytoskeleton. Analysis of these cells allowed stiffening responses to agonists, measured on single cells, to be resolved into an regulatory light chain-mediated component reflecting activation of motor function, and a myosin heavy chain phosphorylation-regulated component reflecting assembly of filaments into the cytoskeleton. These two components can account for all of the cortical stiffening response seen during tested in vivo contractile events.

PMID:
8793728
DOI:
10.1007/bf00124248
[Indexed for MEDLINE]

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