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From the same journal

IPIP27 coordinates PtdIns(4,5)P2 homeostasis for successful cytokinesis

Research output: Contribution to journalArticle

Author(s)

  • Sabrya C. Carim
  • Khaled Ben El Kadhi
  • Guanhua Yan
  • Sean Sweeney
  • Gilles R. Hickson
  • Sebastien Carreno
  • Martin Lowe

Department/unit(s)

Publication details

JournalCurrent Biology
DateAccepted/In press - 22 Dec 2018
DateE-pub ahead of print (current) - 21 Feb 2019
Early online date21/02/19
Original languageEnglish

Abstract

During cytokinesis, an actomyosin contractile ring drives the separation of the two daughter cells. A key molecule in this process is the inositol lipid PtdIns(4,5)P2, which recruits numerous factors to the equatorial region for contractile ring assembly. Despite the importance of PtdIns(4,5)P2 in cytokinesis, the regulation of this lipid in cell division remains poorly understood. Here we identify a role for IPIP27 in mediating cellular PtdIns(4,5)P2 homeostasis. IPIP27 scaffolds the inositol phosphatase OCRL by coupling it to endocytic BAR domain proteins. Loss of IPIP27 causes accumulation of PtdIns(4,5)P2 on aberrant endomembrane vacuoles, mislocalization of the cytokinetic machinery, and extensive cortical membrane blebbing. This phenotype is observed in Drosophilaand human cells, and can result in cytokinesis failure. We have therefore identified IPIP27 as a key modulator of cellular PtdIns(4,5)P2 homeostasisrequired for normal cytokinesis. The results indicate that scaffolding of inositol phosphatase activity is critical for maintaining PtdIns(4,5)P2 homeostasis, and highlight a critical role for this process in cell division.

Bibliographical note

© 2019 The Author(s

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