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Visualizing the Structural Progression of Clathrin Mediated Endocytosis with Fluorescence and Electron Microscopy

Published online by Cambridge University Press:  30 July 2020

Kem Sochacki
Affiliation:
National Institutes of Health, Bethesda, Maryland, United States
John Jimah
Affiliation:
National Institutes of Health, Bethesda, Maryland, United States
Jenny Hinshaw
Affiliation:
National Institutes of Health, Bethesda, Maryland, United States
Justin Taraska
Affiliation:
National Institutes of Health, Bethesda, Maryland, United States

Abstract

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Type
3D Structures: From Macromolecular Assemblies to Whole Cells (3DEM FIG)
Copyright
Copyright © Microscopy Society of America 2020

References

Sochacki, K.A. and Taraska, J.W., From Flat to Curved Clathrin: Controlling a Plastic Ratchet. Trends in cell biology, 2018.Google ScholarPubMed
Scott, B.L., Sochacki, K.A., Low-Nam, S.T., Bailey, E.M., Luu, Q., Hor, A., Dickey, A.M., Smith, S., Kerkvliet, J.G., and Taraska, J.W., Membrane bending occurs at all stages of clathrin-coat assembly and defines endocytic dynamics. Nature communications, 2018. 9(1): p. 419.10.1038/s41467-018-02818-8CrossRefGoogle ScholarPubMed
Bucher, D., Frey, F., Sochacki, K.A., Kummer, S., Bergeest, J.-P., Godinez, W.J., Kräusslich, H.-G., Rohr, K., Taraska, J.W., and Schwarz, U.S., Clathrin-adaptor ratio and membrane tension regulate the flat-to-curved transition of the clathrin coat during endocytosis. Nature communications, 2018. 9(1): p. 1109.10.1038/s41467-018-03533-0CrossRefGoogle ScholarPubMed
Avinoam, O., Schorb, M., Beese, C.J., Briggs, J.A., and Kaksonen, M., ENDOCYTOSIS. Endocytic sites mature by continuous bending and remodeling of the clathrin coat. Science, 2015. 348(6241): p. 1369-72.10.1126/science.aaa9555CrossRefGoogle ScholarPubMed
Morris, K.L., Jones, J.R., Halebian, M., Wu, S., Baker, M., Armache, J.-P., Ibarra, A.A., Sessions, R.B., Cameron, A.D., and Cheng, Y., Cryo-EM of multiple cage architectures reveals a universal mode of clathrin self-assembly. Nature structural & molecular biology, 2019. 26(10): p. 890-898.Google Scholar
Sochacki, K.A., Shtengel, G., Van Engelenburg, S.B., Hess, H.F., and Taraska, J.W., Correlative super-resolution fluorescence and metal-replica transmission electron microscopy. Nature methods, 2014. 11(3): p. 305.10.1038/nmeth.2816CrossRefGoogle ScholarPubMed
Sochacki, K.A. and Taraska, J.W., Correlative fluorescence super-resolution localization microscopy and platinum replica EM on unroofed cells, in Super-Resolution Microscopy. 2017, Springer. p. 219-230.10.1007/978-1-4939-7265-4_18CrossRefGoogle Scholar
Sochacki, K.A., Dickey, A.M., Strub, M.-P., and Taraska, J.W., Endocytic proteins are partitioned at the edge of the clathrin lattice in mammalian cells. Nature cell biology, 2017. 19(4): p. 352.10.1038/ncb3498CrossRefGoogle Scholar