Cytokinesis mediated through the recruitment of cortexillins into the cleavage furrow

Research output: Contribution to journalArticle

  • External authors:
  • Igor Weber
  • Günther Gerisch
  • Christina Heizer
  • John Murphy
  • Kim Badelt
  • Alexander Stock
  • Jan Faix


The fact that substrate-anchored Dictyostelium cells undergo cytokinesis in the absence of myosin II underscores the importance of other proteins in enabling the cleavage furrow to constrict. Cortexillins, a pair of actin-bundling proteins, are required for normal cleavage. They are targeted to the incipient furrow in wild-type and, more prominently, in myosin II-null cells. No other F-actin bundling or cross-linking protein tested is co-localized. Green fluorescent protein fusions show that the N-terminal actin-binding domain of cortexillin I is dispensable and the C-terminal region is sufficient for translocation to the furrow and the rescue of cytokinesis. Cortexillins are suggested to have a targeting signal for coupling to a myosin II-independent system that directs transport of membrane proteins to the cleavage furrow.

Bibliographical metadata

Original languageEnglish
Pages (from-to)586-594
Number of pages8
JournalEMBO Journal
Issue number3
Publication statusPublished - 1 Feb 1999