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

Laure Plantard, Antti Arjonen, John G. Lock, Ghasem Nurani, Johanna Ivaska, Staffan Strömblad

Research output: Contribution to journalArticleScientificpeer-review

44 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)3525-3534
JournalJournal of Cell Science
Volume123
Issue number20
DOIs
Publication statusPublished - 2010
MoE publication typeA1 Journal article-refereed

Fingerprint

Pseudopodia
Myosins
Microtubules
Cell Movement
phosphatidylinositol 3,4,5-triphosphate
Membrane Proteins

Keywords

  • Endosome
  • Filopodia
  • Myosin-X
  • PH domain
  • PtdIns(3,4,5)P3

Cite this

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(20), 3525-3534. https://doi.org/10.1242/jcs.069609
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. 20. pp. 3525-3534.
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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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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. 20, pp. 3525-3534. https://doi.org/10.1242/jcs.069609

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. 20, 2010, p. 3525-3534.

Research output: Contribution to journalArticleScientificpeer-review

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

Y1 - 2010

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.

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KW - Filopodia

KW - Myosin-X

KW - PH domain

KW - PtdIns(3,4,5)P3

U2 - 10.1242/jcs.069609

DO - 10.1242/jcs.069609

M3 - Article

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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;123(20):3525-3534. https://doi.org/10.1242/jcs.069609