Dictyostelium mutants lacking the cytoskeletal protein coronin are defective in cytokinesis and cell motility.

DOI PDF 被引用文献16件
  • E L de Hostos
    Max-Planck-Institut für Biochemie, Martinsried, Germany.
  • C Rehfuess
    Max-Planck-Institut für Biochemie, Martinsried, Germany.
  • B Bradtke
    Max-Planck-Institut für Biochemie, Martinsried, Germany.
  • D R Waddell
    Max-Planck-Institut für Biochemie, Martinsried, Germany.
  • R Albrecht
    Max-Planck-Institut für Biochemie, Martinsried, Germany.
  • J Murphy
    Max-Planck-Institut für Biochemie, Martinsried, Germany.
  • G Gerisch
    Max-Planck-Institut für Biochemie, Martinsried, Germany.

抄録

<jats:p>Coronin is an actin-binding protein in Dictyostelium discoideum that is enriched at the leading edge of the cells and in projections of the cell surface called crowns. The polypeptide sequence of coronin is distinguished by its similarities to the beta-subunits of trimeric G proteins (E. L. de Hostos, B. Bradtke, F. Lottspeich, R. Guggenheim, and G. Gerisch, 1991. EMBO (Eur. Mol. Biol. Organ.) J. 10:4097-4104). To elucidate the in vivo function of coronin, null mutants have been generated by gene replacement. The mutant cells lacking coronin grow and migrate more slowly than wild-type cells. When these cor- cells grow in liquid medium they become multinucleate, indicating a role of coronin in cytokinesis. To explore this role, coronin has been localized in mitotic wild-type cells by immunofluorescence labeling. During separation of the daughter cells, coronin is strongly accumulated at their distal portions including the leading edges. This contrasts with the localization of myosin II in the cleavage furrow and suggests that coronin functions independently of the conventional myosin in facilitating cytokinesis.</jats:p>

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