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Updated: Jun 8, 2026

Radiolabeling and Quantification of Cellular Levels of Phosphoinositides by High Performance Liquid Chromatography-coupled Flow Scintillation
Published on: January 6, 2016
PtdIns(3,4,5)P₃ is a regulator of myosin-X localization and filopodia formation
Laure Plantard1, Antti Arjonen, John G Lock
1Center for Biosciences, Department of Biosciences and Nutrition, Karolinska Institutet, 14183 Huddinge, Sweden.
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.
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