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

Thomas T. Egelhoff, Teresa V. Naismith, Frank V. Brozovich

Research output: Contribution to journalArticle

32 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)269-274
Number of pages6
JournalJournal of Muscle Research and Cell Motility
Volume17
Issue number2
DOIs
StatePublished - 1996

ASJC Scopus subject areas

  • Biochemistry
  • Physiology
  • Cell Biology

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