4.5 Article

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

Journal

JOURNAL OF CELL SCIENCE
Volume 123, Issue 20, Pages 3525-3534

Publisher

COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.069609

Keywords

Endosome; Filopodia; Myosin-X; PH domain; PtdIns(3,4,5)P-3

Categories

Funding

  1. Swedish Cancer Society
  2. Swedish Research Council
  3. Center for Biosciences at Karolinska Institutet
  4. ERC
  5. Academy of Finland
  6. Sigrid Juselius Foundation
  7. Finnish Cancer Organizations
  8. EMBO
  9. Emil Aaltonen foundation
  10. Pertelin Aaltonen foundation
  11. Maud Kuistila foundation
  12. TUBS Graduate School
  13. Knut and Alice Wallenberg Foundation
  14. Center for Biosciences

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Phosphatidylinositol (3,4,5)-trisphosphate [PtdIns(3,4,5)P-3] 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)P-3 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)P-3, 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)P-3-binding, our results indicate that PtdIns(3,4,5)P-3 binding to the Myo10-PH2 domain is involved in Myo10 trafficking and regulation of filopodia dynamics.

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