The DOI matches its Crossref record; 44 of the 44 references it cites were found in a registry or an index.
An actin-dependent mechanism for long-range vesicle transport
Open accessAbstract
Intracellular transport is vital for the function, survival and architecture of every eukaryotic cell. Long-range transport in animal cells is thought to depend exclusively on microtubule tracks. This study reveals an unexpected actin-dependent but microtubule-independent mechanism for long-range transport of vesicles. Vesicles organize their own actin tracks by recruiting the actin nucleation factors Spire1, Spire2 and Formin-2, which assemble an extensive actin network from the vesicles’ surfaces. The network connects the vesicles with one another and with the plasma membrane. Vesicles move directionally along these connections in a myosin-Vb-dependent manner to converge and to reach the cell surface. The overall outward-directed movement of the vesicle-actin network is driven by recruitment of vesicles to the plasma membrane in the periphery of the oocyte. Being organized in a dynamic vesicle-actin network allows vesicles to move in a local random manner and a global directed manner at the same time: they can reach any position in the cytoplasm, but also move directionally to the cell surface as a collective. Thus, collective movement within a network is a powerful and flexible mode of vesicle transport.
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Cites
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Rab GTPases as coordinators of vesicle traffic
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Kinesin superfamily motor proteins and intracellular transport
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“Accordingly, the minus-end-directed motor protein dynein mediates transport to the cell centre, and plus-end-directed kinesins mediate transport to the peripher”
BackgroundPathways and mechanisms of endocytic recycling
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Subunit stoichiometry of a mammalian K+ channel determined by construction of multimeric cDNAs
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Cited by
Delon, L. C., Guo, Z., Oszmiana, A., Chien, C.-C., Gibson, R., Prestidge, C., & Thierry, B. (2019) · Biomaterials · doi:10.1016/j.biomaterials.2019.119521 · Cited by 171
Actin-dependent endosomal receptor recycling
Simonetti, B., & Cullen, P. J. (2019) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2018.08.006 · Cited by 139
Martin, L., Kaci, N., Estibals, V., Goudin, N., Garfa-Traore, M., Benoist-Lasselin, C., Dambroise, E., & Legeai-Mallet, L. (2018) · Human Molecular Genetics · doi:10.1093/hmg/ddx374 · Cited by 51
Dynamin 2 regulates biphasic insulin secretion and plasma glucose homeostasis
Fan, F., Ji, C., Wu, Y., Ferguson, S. M., Tamarina, N., Philipson, L. H., & Lou, X. (2015) · Journal of Clinical Investigation · doi:10.1172/jci80652 · Cited by 43
Conrad, R., Stölting, G., Hendriks, J., Ruello, G., Kortzak, D., Jordan, N., Gensch, T., & Hidalgo, P. (2018) · iScience · doi:10.1016/j.isci.2018.08.012 · Cited by 35
Metadata
- Authors
- Schuh, M.
- Venue
- Nature Cell Biology
- Published
- 2011-10-09
- Volume
- 13
- Issue
- 12
- Pages
- 1431-1436
- ISSN
- 1465-7392 (ISSN-L)
- 1476-4679
- OpenAlex
- W1992885630
- Cited by
- 324
- References
- 44
- FWCI
- 9.80
- Type
- journal article
- Language
- en
- Open access
- green
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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