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Phosphatidylinositol(4,5)bisphosphate coordinates actin-mediated mobilization and translocation of secretory vesicles to the plasma membrane of chromaffin cells

Author

Listed:
  • Peter J. Wen

    (The University of Queensland, Queensland Brain Institute and School of Biomedical Sciences)

  • Shona L. Osborne

    (The University of Queensland, Queensland Brain Institute and School of Biomedical Sciences)

  • Mark Zanin

    (Flinders University)

  • Pei Ching Low

    (The University of Queensland, Queensland Brain Institute and School of Biomedical Sciences)

  • Hai-Tao A. Wang

    (The University of Queensland, Queensland Brain Institute and School of Biomedical Sciences)

  • Simone M. Schoenwaelder

    (Australian Centre for Blood Diseases, Monash University, Alfred Medical Research and Education Precinct)

  • Shaun P. Jackson

    (Australian Centre for Blood Diseases, Monash University, Alfred Medical Research and Education Precinct)

  • Roland Wedlich-Söldner

    (Max Planck Institute of Biochemistry, Research Group Cellular Dynamics and Cell Patterning)

  • Bart Vanhaesebroeck

    (Centre for Cell Signalling, Barts Cancer Institute, Queen Mary University of London)

  • Damien J. Keating

    (Flinders University)

  • Frédéric A. Meunier

    (The University of Queensland, Queensland Brain Institute and School of Biomedical Sciences)

Abstract

Neurosecretory vesicles undergo docking and priming before Ca2+-dependent fusion with the plasma membrane. Although de novo synthesis of phosphatidylinositol(4,5)bisphosphate (PtdIns(4,5)P2) is required for exocytosis, its precise contribution is still unclear. Here we show that inhibition of the p110δ isoform of PI3-kinase by IC87114 promotes a transient increase in PtdIns(4,5)P2, leading to a potentiation of exocytosis in chromaffin cells. We then exploit this pathway to examine the effect of a transient PtdIns(4,5)P2 increase on neurosecretory vesicles behaviour, outside the context of a secretagogue stimulation. Our results demonstrate that a rise in PtdIns(4,5)P2 is sufficient to promote the mobilization and recruitment of secretory vesicles to the plasma membrane via Cdc42-mediated actin reorganization. PtdIns(4,5)P2, therefore, orchestrates the actin-based conveyance of secretory vesicles to the plasma membrane.

Suggested Citation

  • Peter J. Wen & Shona L. Osborne & Mark Zanin & Pei Ching Low & Hai-Tao A. Wang & Simone M. Schoenwaelder & Shaun P. Jackson & Roland Wedlich-Söldner & Bart Vanhaesebroeck & Damien J. Keating & Frédéri, 2011. "Phosphatidylinositol(4,5)bisphosphate coordinates actin-mediated mobilization and translocation of secretory vesicles to the plasma membrane of chromaffin cells," Nature Communications, Nature, vol. 2(1), pages 1-11, September.
    • Handle: RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1500
    DOI: 10.1038/ncomms1500
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    Cited by:

    1. Anmin Jiang & Kye Kudo & Rachel S. Gormal & Sevannah Ellis & Sikao Guo & Tristan P. Wallis & Shanley F. Longfield & Phillip J. Robinson & Margaret E. Johnson & Merja Joensuu & Frédéric A. Meunier, 2024. "Dynamin1 long- and short-tail isoforms exploit distinct recruitment and spatial patterns to form endocytic nanoclusters," Nature Communications, Nature, vol. 15(1), pages 1-21, December.

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