PtdIns(3,4,5)P3 is a regulator of myosin-X localization and filopodia formation
Research output: Contribution to journal › Journal article › Research › peer-review
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 language | English |
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Journal | Journal of Cell Science |
Volume | 123 |
Issue number | Pt 20 |
Pages (from-to) | 3525-34 |
Number of pages | 10 |
ISSN | 0021-9533 |
DOIs | |
Publication status | Published - 15 Oct 2010 |
- Animals, COS Cells, Cercopithecus aethiops, Endosomes, HeLa Cells, Humans, Immunoprecipitation, Myosins, Phosphatidylinositol Phosphates, Protein Binding, Protein Structure, Tertiary, Pseudopodia
Research areas
ID: 45161498