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

Alzahofi, Noura; Welz, Tobias; Robinson, Christopher L.; Page, Emma L.; Briggs, Deborah A.; Stainthorp, Amy K.; Reekes, James; Elbe, David A.; Straub, Felix; Kallemeijn, Wouter W.; Tate, Edward W.; Goff, Philip S.; Sviderskaya, Elena V.; Cantero, Marta; Montoliu, Lluis; Nedelec, Francois; Miles, Amanda K.; Bailly, Maryse; Kerkhoff, Eugen; Hume, Alistair N.

Abstract

© 2020, The Author(s). 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.

Citation

Alzahofi, N., Welz, T., Robinson, C. L., Page, E. L., Briggs, D. A., Stainthorp, A. K., Reekes, J., Elbe, D. A., Straub, F., Kallemeijn, W. W., Tate, E. W., Goff, P. S., Sviderskaya, E. V., Cantero, M., Montoliu, L., Nedelec, F., Miles, A. K., Bailly, M., Kerkhoff, E., & Hume, A. N. (2020). Rab27a co-ordinates actin-dependent transport by controlling organelle-associated motors and track assembly proteins. Nature Communications, 11(1), Article 3495. https://doi.org/10.1038/s41467-020-17212-6

• Journal Article Type: Article
• Acceptance Date: Jun 4, 2020
• Online Publication Date: Jul 13, 2020
• Publication Date: Dec 1, 2020
• Deposit Date: Jun 10, 2020
• Publicly Available Date: Jul 13, 2020
• Journal: Nature Communications
• Electronic ISSN: 2041-1723
• Publisher: Nature Publishing Group
• Peer Reviewed: Peer Reviewed
• Volume: 11
• Issue: 1
• Article Number: 3495
• DOI: https://doi.org/10.1038/s41467-020-17212-6
• Keywords: General Biochemistry, Genetics and Molecular Biology; General Physics and Astronomy; General Chemistry
• Public URL: https://nottingham-repository.worktribe.com/output/4618770
• Publisher URL: https://www.nature.com/articles/s41467-020-17212-6