Journal
JOURNAL OF CELL SCIENCE
Volume 123, Issue 20, Pages 3525-3534Publisher
COMPANY OF BIOLOGISTS LTD
DOI: 10.1242/jcs.069609
Keywords
Endosome; Filopodia; Myosin-X; PH domain; PtdIns(3,4,5)P-3
Categories
Funding
- Swedish Cancer Society
- Swedish Research Council
- Center for Biosciences at Karolinska Institutet
- ERC
- Academy of Finland
- Sigrid Juselius Foundation
- Finnish Cancer Organizations
- EMBO
- Emil Aaltonen foundation
- Pertelin Aaltonen foundation
- Maud Kuistila foundation
- TUBS Graduate School
- Knut and Alice Wallenberg Foundation
- Center for Biosciences
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available