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Rab27a co-ordinates actin-dependent transport by controlling organelle-associated motors and track assembly proteins

Author

Listed:
  • Noura Alzahofi

    (University of Nottingham)

  • Tobias Welz

    (University Hospital Regensburg)

  • Christopher L. Robinson

    (University of Nottingham)

  • Emma L. Page

    (University of Nottingham)

  • Deborah A. Briggs

    (University of Nottingham)

  • Amy K. Stainthorp

    (University of Nottingham)

  • James Reekes

    (University of Nottingham)

  • David A. Elbe

    (University of Nottingham)

  • Felix Straub

    (University Hospital Regensburg)

  • Wouter W. Kallemeijn

    (Imperial College London, Molecular Sciences Research Hub)

  • Edward W. Tate

    (Imperial College London, Molecular Sciences Research Hub)

  • Philip S. Goff

    (St. George’s, University of London)

  • Elena V. Sviderskaya

    (St. George’s, University of London)

  • Marta Cantero

    (Centro Nacional de Biotecnologia (CNB-CSIC)
    CIBERER-ISCIII)

  • Lluis Montoliu

    (Centro Nacional de Biotecnologia (CNB-CSIC)
    CIBERER-ISCIII)

  • Francois Nedelec

    (Cambridge University)

  • Amanda K. Miles

    (Nottingham Trent University)

  • Maryse Bailly

    (UCL Institute of Ophthalmology)

  • Eugen Kerkhoff

    (University Hospital Regensburg)

  • Alistair N. Hume

    (University of Nottingham)

Abstract

Cell biologists generally consider that microtubules and actin play complementary roles in long- and short-distance transport in animal cells. On the contrary, using melanosomes of melanocytes as a model, we recently discovered that the motor protein myosin-Va works with dynamic actin tracks to drive long-range organelle dispersion in opposition to microtubules. This suggests that in animals, as in yeast and plants, myosin/actin can drive long-range transport. Here, we show that the SPIRE-type actin nucleators (predominantly SPIRE1) are Rab27a effectors that co-operate with formin-1 to generate actin tracks required for myosin-Va-dependent transport in melanocytes. Thus, in addition to melanophilin/myosin-Va, Rab27a can recruit SPIREs to melanosomes, thereby integrating motor and track assembly activity at the organelle membrane. Based on this, we suggest a model in which organelles and force generators (motors and track assemblers) are linked, forming an organelle-based, cell-wide network that allows their collective activity to rapidly disperse the population of organelles long-distance throughout the cytoplasm.

Suggested Citation

  • Noura Alzahofi & Tobias Welz & Christopher L. Robinson & Emma L. Page & Deborah A. Briggs & Amy K. Stainthorp & James Reekes & David A. Elbe & Felix Straub & Wouter W. Kallemeijn & Edward W. Tate & Ph, 2020. "Rab27a co-ordinates actin-dependent transport by controlling organelle-associated motors and track assembly proteins," Nature Communications, Nature, vol. 11(1), pages 1-21, December.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-17212-6
    DOI: 10.1038/s41467-020-17212-6
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    References listed on IDEAS

    as
    1. Margot E. Quinlan & John E. Heuser & Eugen Kerkhoff & R. Dyche Mullins, 2005. "Drosophila Spire is an actin nucleation factor," Nature, Nature, vol. 433(7024), pages 382-388, January.
    2. Takanori Otomo & Diana R. Tomchick & Chinatsu Otomo & Sanjay C. Panchal & Mischa Machius & Michael K. Rosen, 2005. "Structural basis of actin filament nucleation and processive capping by a formin homology 2 domain," Nature, Nature, vol. 433(7025), pages 488-494, February.
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