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

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 and Frédéric A. Meunier ()
Additional contact information
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

Nature Communications, 2011, vol. 2, issue 1, 1-11

Abstract: 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.

Date: 2011
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/ncomms1500 Abstract (text/html)

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:2:y:2011:i:1:d:10.1038_ncomms1500

Ordering information: This journal article can be ordered from
https://www.nature.com/ncomms/

DOI: 10.1038/ncomms1500

Access Statistics for this article

Nature Communications is currently edited by Nathalie Le Bot, Enda Bergin and Fiona Gillespie

More articles in Nature Communications from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().