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

Standard

PtdIns(3,4,5)P3 is a regulator of myosin-X localization and filopodia formation. / Plantard, Laure; Arjonen, Antti; Lock, John G; Nurani, Ghasem; Ivaska, Johanna; Strömblad, Staffan.

In: Journal of Cell Science, Vol. 123, No. Pt 20, 15.10.2010, p. 3525-34.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Plantard, L, Arjonen, A, Lock, JG, 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, vol. 123, no. Pt 20, pp. 3525-34. https://doi.org/10.1242/jcs.069609

APA

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(Pt 20), 3525-34. https://doi.org/10.1242/jcs.069609

Vancouver

Plantard L, Arjonen A, Lock JG, Nurani G, Ivaska J, Strömblad S. PtdIns(3,4,5)P3 is a regulator of myosin-X localization and filopodia formation. Journal of Cell Science. 2010 Oct 15;123(Pt 20):3525-34. https://doi.org/10.1242/jcs.069609

Author

Plantard, Laure ; Arjonen, Antti ; Lock, John G ; Nurani, Ghasem ; Ivaska, Johanna ; Strömblad, Staffan. / PtdIns(3,4,5)P3 is a regulator of myosin-X localization and filopodia formation. In: Journal of Cell Science. 2010 ; Vol. 123, No. Pt 20. pp. 3525-34.

Bibtex

@article{68d4c0ca469c4a549c99cae6916b5b5b,
title = "PtdIns(3,4,5)P3 is a regulator of myosin-X localization and filopodia formation",
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.",
keywords = "Animals, COS Cells, Cercopithecus aethiops, Endosomes, HeLa Cells, Humans, Immunoprecipitation, Myosins, Phosphatidylinositol Phosphates, Protein Binding, Protein Structure, Tertiary, Pseudopodia",
author = "Laure Plantard and Antti Arjonen and Lock, {John G} and Ghasem Nurani and Johanna Ivaska and Staffan Str{\"o}mblad",
year = "2010",
month = oct,
day = "15",
doi = "10.1242/jcs.069609",
language = "English",
volume = "123",
pages = "3525--34",
journal = "Journal of Cell Science",
issn = "0021-9533",
publisher = "The/Company of Biologists Ltd.",
number = "Pt 20",

}

RIS

TY - JOUR

T1 - PtdIns(3,4,5)P3 is a regulator of myosin-X localization and filopodia formation

AU - Plantard, Laure

AU - Arjonen, Antti

AU - Lock, John G

AU - Nurani, Ghasem

AU - Ivaska, Johanna

AU - Strömblad, Staffan

PY - 2010/10/15

Y1 - 2010/10/15

N2 - 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.

AB - 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.

KW - Animals

KW - COS Cells

KW - Cercopithecus aethiops

KW - Endosomes

KW - HeLa Cells

KW - Humans

KW - Immunoprecipitation

KW - Myosins

KW - Phosphatidylinositol Phosphates

KW - Protein Binding

KW - Protein Structure, Tertiary

KW - Pseudopodia

U2 - 10.1242/jcs.069609

DO - 10.1242/jcs.069609

M3 - Journal article

C2 - 20930142

VL - 123

SP - 3525

EP - 3534

JO - Journal of Cell Science

JF - Journal of Cell Science

SN - 0021-9533

IS - Pt 20

ER -

ID: 45161498