Sequential Cyk-4 binding to ECT2 and FIP3 regulates cleavage furrow ingression and abscission during cytokinesis

Glenn C. Simon, Eric Schonteich, Christine C. Wu, Alisa Piekny, Damian Ekiert, Xinzi Yu, Gwyn W. Gould, Michael Glotzer, Rytis Prekeris

Research output: Contribution to journalArticle

67 Citations (Scopus)

Abstract

Cytokinesis is a highly regulated and dynamic event that involves the reorganization of the cytoskeleton and membrane compartments. Recently, FIP3 has been implicated in targeting of recycling endosomes to the mid-body of dividing cells and is found required for abscission. Here, we demonstrate that the centralspindlin component Cyk-4 is a FIP3-binding protein. Furthermore, we show that FIP3 binds to Cyk-4 at late telophase and that centralspindlin may be required for FIP3 recruitment to the mid-body. We have mapped the FIP3-binding region on Cyk-4 and show that it overlaps with the ECT2-binding domain. Finally, we demonstrate that FIP3 and ECT2 form mutually exclusive complexes with Cyk-4 and that dissociation of ECT2 from the mid-body at late telophase may be required for the recruitment of FIP3 and recycling endosomes to the cleavage furrow. Thus, we propose that centralspindlin complex not only regulates acto-myosin ring contraction but also endocytic vesicle transport to the cleavage furrow and it does so through sequential interactions with ECT2 and FIP3.

Original languageEnglish
Pages (from-to)1791-1803
Number of pages13
JournalEMBO Journal
Volume27
Issue number13
Early online date29 May 2008
DOIs
Publication statusPublished - 9 Jul 2008

Keywords

  • Cyk-4
  • Cytokinesis
  • Endosomes
  • FIP3
  • Rab11
  • cell biology
  • mitosis

Fingerprint Dive into the research topics of 'Sequential Cyk-4 binding to ECT2 and FIP3 regulates cleavage furrow ingression and abscission during cytokinesis'. Together they form a unique fingerprint.

Cite this