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Arp2/3-mediated F-actin formation controls regulated exocytosis in vivo

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  • Duy T. Tran

    (Developmental Glycobiology Section, NIDCR, National Institutes of Health, Building 30, Room 426, 30 Convent Drive, MSC 4370, Bethesda, Maryland 20892, USA)

  • Andrius Masedunskas

    (Intracellular Membrane Trafficking Section, NIDCR, National Institutes of Health, 30 Convent Drive, Bethesda, Maryland 20892, USA
    Oncology Research Unit, School of Medical Sciences, University of New South Wales)

  • Roberto Weigert

    (Intracellular Membrane Trafficking Section, NIDCR, National Institutes of Health, 30 Convent Drive, Bethesda, Maryland 20892, USA)

  • Kelly G. Ten Hagen

    (Developmental Glycobiology Section, NIDCR, National Institutes of Health, Building 30, Room 426, 30 Convent Drive, MSC 4370, Bethesda, Maryland 20892, USA)

Abstract

The actin cytoskeleton plays crucial roles in many cellular processes, including regulated secretion. However, the mechanisms controlling F-actin dynamics in this process are largely unknown. Through 3D time-lapse imaging in a secreting organ, we show that F-actin is actively disassembled along the apical plasma membrane at the site of secretory vesicle fusion and re-assembled directionally on vesicle membranes. Moreover, we show that fusion pore formation and PIP2 redistribution precedes actin and myosin recruitment to secretory vesicle membranes. Finally, we show essential roles for the branched actin nucleators Arp2/3- and WASp in the process of secretory cargo expulsion and integration of vesicular membranes with the apical plasma membrane. Our results highlight previously unknown roles for branched actin in exocytosis and provide a genetically tractable system to image the temporal and spatial dynamics of polarized secretion in vivo.

Suggested Citation

  • Duy T. Tran & Andrius Masedunskas & Roberto Weigert & Kelly G. Ten Hagen, 2015. "Arp2/3-mediated F-actin formation controls regulated exocytosis in vivo," Nature Communications, Nature, vol. 6(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:6:y:2015:i:1:d:10.1038_ncomms10098
    DOI: 10.1038/ncomms10098
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