PtdIns(3,4,5)P3 is a regulator of myosin-X localization and filopodia formation

Laure Plantard, Antti Arjonen, John G. Lock, Ghasem Nurani, Johanna Ivaska, Staffan Strömblad

Research output: Contribution to journalArticleScientificpeer-review

53 Citations (Scopus)

Abstract

Phosphatidylinositol (3,4,5)-trisphosphate [PtdIns(3,4,5)P3] is a key regulator of cell signaling that acts by recruiting proteins to the cell membrane, such as at the leading edge during cell migration. Here, we show that PtdIns (3,4,5)P3 plays a central role in filopodia formation via the binding of myosin-X (Myo10), a potent promoter of filopodia. We found that the second pleckstrin homology domain (Myo10-PH2) of Myo10 specifically binds to PtdIns(3,4,5)P3, and that disruption of this binding led to impairment of filopodia and partial re-localization of Myo10 to microtubule-associated Rab7-positive endosomal vesicles. Given that the localization of Myo10 was dynamically restored to filopodia upon reinstatement of PtdIns(3,4,5)P3-binding, our results indicate that PtdIns(3,4,5)P3 binding to the Myo10-PH2 domain is involved in Myo10 trafficking and regulation of filopodia dynamics.
Original languageEnglish
Pages (from-to)3525-3534
JournalJournal of Cell Science
Volume123
Issue number20
DOIs
Publication statusPublished - 2010
MoE publication typeA1 Journal article-refereed

Keywords

  • Endosome
  • Filopodia
  • Myosin-X
  • PH domain
  • PtdIns(3,4,5)P3

Fingerprint Dive into the research topics of 'PtdIns(3,4,5)P<sub>3</sub> is a regulator of myosin-X localization and filopodia formation'. Together they form a unique fingerprint.

Cite this