An unconventional myosin required for cell polarization and chemotaxis

Laura M. Breshears, Deborah Wessels, David R. Soll, Margaret A. Titus

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

MyTH/FERM (myosin tail homology 4/band 4.1, ezrin, radixin, and moesin) myosins have roles in cellular adhesion, extension of actin-filled projections such as filopodia and stereocilia, and directional migration. The amoeba Dictyostelium discoideum expresses a simple complement of MyTH/FERM myosins, a class VII (M7) myosin required for cell-substrate adhesion and a unique myosin named MyoG. Mutants lacking MyoG exhibit a wide range of normal actin-based behaviors, including chemotaxis to folic acid, but have a striking defect in polarization and chemotaxis to cAMP. Although the myoG mutants respond to cAMP stimulation by increasing persistence and weakly increasing levels of cortical F-actin, they do not polarize; instead, they maintain a round shape and move slowly and randomly when exposed to a chemotactic gradient. The mutants also fail to activate and localize PI3K to the membrane closest to the source of chemoattractant. These data reveal a role for a MyTH/FERM myosin in mediating early chemotactic signaling and suggest that MyTH/FERM proteins have conserved roles in signaling and the generation of cell polarity.

Original languageEnglish (US)
Pages (from-to)6918-6923
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume107
Issue number15
DOIs
StatePublished - Apr 13 2010

Keywords

  • Actin cytoskeleton
  • Cell motility
  • Cell signaling
  • Cytoskeletal dynamics

Fingerprint Dive into the research topics of 'An unconventional myosin required for cell polarization and chemotaxis'. Together they form a unique fingerprint.

Cite this