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

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49 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

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    Plantard, L., Arjonen, A., Lock, J. G., Nurani, G., Ivaska, J., & Strömblad, S. (2010). PtdIns(3,4,5)P3 is a regulator of myosin-X localization and filopodia formation. Journal of Cell Science, 123(20), 3525-3534. https://doi.org/10.1242/jcs.069609