The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
Structural Organization of the Actin Cytoskeleton at Sites of Clathrin-Mediated Endocytosis
Open accessAbstract
SUMMARY Background The dynamic actin cytoskeleton plays an important role in clathrin-mediated endocytosis (CME). However, its exact functions remain uncertain due to a lack of high resolution structural information regarding actin architecture at endocytic sites. Results Using platinum replica electron microscopy in combination with electron tomography we found that actin patches associated with clathrin-coated structures (CCSs) in cultured mouse cells consist of a densely branched actin network, in which actin filament barbed ends are oriented toward the CCS. The shape of the actin network varied from a small lateral patch at the periphery of shallow CCSs, to a collar-like arrangement around partly invaginated CCSs with actin filament barbed ends abutting the CCS neck, to a polarized comet tail in association with highly constricted or fully endocytosed CCSs. Conclusions Our data suggest that the primary role of the actin cytoskeleton in CME is to constrict and elongate the bud neck and drive the endocytosed vesicles from the plasma membrane. Moreover, in these processes barbed ends directly push onto the load, as in a conventional propulsion mechanism. Based on our findings we propose a model for initiation, evolution, and function of the dendritic actin network at CCSs.
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Cites
Scar, a WASp-related protein, activates nucleation of actin filaments by the Arp2/3 complex
Machesky, L. M., Mullins, R. D., Higgs, H. N., Kaiser, D. A., Blanchoin, L., May, R. C., Hall, M. E., & Pollard, T. D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.7.3739 · Cited by 773
Merrifield, C. J., Perrais, D., & Zenisek, D. (2005) · Cell · doi:10.1016/j.cell.2005.03.015 · Cited by 476 · cited 2×
“Actin polymerization was proposed to function at multiple stages of CME, including formation, invagination, constriction, and lateral movement of clathrin-coated pits, as well as scission and departure of clathrin-coated vesicles [3, 5–7, 28–30].”
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Ferguson, S. M., & De Camilli, P. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3266 · Cited by 992
The actin cytoskeleton and actin-based motility
Svitkina, T. (2018) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018267 · Cited by 761
Self-citationCorrelated light and electron microscopy: ultrastructure lights up!
de Boer, P., Hoogenboom, J. P., & Giepmans, B. N. G. (2015) · Nature Methods · doi:10.1038/nmeth.3400 · Cited by 526
Video-rate nanoscopy using sCMOS camera–specific single-molecule localization algorithms
Huang, F., Hartwich, T. M. P., Rivera-Molina, F. E., Lin, Y., Duim, W. C., Long, J. J., Uchil, P. D., Myers, J. R., Baird, M. A., Mothes, W., et al. (2013) · Nature Methods · doi:10.1038/nmeth.2488 · Cited by 526
Metadata
- Authors
- Collins, A., Warrington, A., Taylor, K. A., & Svitkina, T.
- Venue
- Current Biology
- Publisher
- Elsevier BV
- Published
- 2011-07
- Volume
- 21
- Issue
- 14
- Pages
- 1167-1175
- ISSN
- 0960-9822 (ISSN-L)
- OpenAlex
- W2049097378
- Cited by
- 243
- References
- 2
- FWCI
- 9.53
- Type
- journal article
- Language
- en
- Open access
- bronze
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