Nanoscale subcellular architecture revealed by multicolor three-dimensional salvaged fluorescence imaging.


Journal

Nature methods
ISSN: 1548-7105
Titre abrégé: Nat Methods
Pays: United States
ID NLM: 101215604

Informations de publication

Date de publication:
02 2020
Historique:
received: 01 05 2019
accepted: 11 11 2019
pubmed: 8 1 2020
medline: 6 5 2020
entrez: 8 1 2020
Statut: ppublish

Résumé

Combining the molecular specificity of fluorescent probes with three-dimensional imaging at nanoscale resolution is critical for investigating the spatial organization and interactions of cellular organelles and protein complexes. We present a 4Pi single-molecule switching super-resolution microscope that enables ratiometric multicolor imaging of mammalian cells at 5-10-nm localization precision in three dimensions using 'salvaged fluorescence'. Imaging two or three fluorophores simultaneously, we show fluorescence images that resolve the highly convoluted Golgi apparatus and the close contacts between the endoplasmic reticulum and the plasma membrane, structures that have traditionally been the imaging realm of electron microscopy. The salvaged fluorescence approach is equally applicable in most single-objective microscopes.

Identifiants

pubmed: 31907447
doi: 10.1038/s41592-019-0676-4
pii: 10.1038/s41592-019-0676-4
pmc: PMC7028321
mid: NIHMS1542660
doi:

Types de publication

Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

IM

Pagination

225-231

Subventions

Organisme : NIGMS NIH HHS
ID : R01 GM118486
Pays : United States
Organisme : NIDDK NIH HHS
ID : P30 DK045735
Pays : United States
Organisme : Wellcome Trust
Pays : United Kingdom
Organisme : NINDS NIH HHS
ID : R37 NS036251
Pays : United States
Organisme : NINDS NIH HHS
ID : R01 NS036251
Pays : United States
Organisme : Wellcome Trust
ID : 203285/Z/16/Z
Pays : United Kingdom

Références

Ladinsky, M. S., Mastronarde, D. N., McIntosh, J. R., Howell, K. E. & Staehelin, L. A. Golgi structure in three dimensions: functional insights from the normal rat kidney cell. J. Cell Biol. 144, 1135–1149 (1999).
pubmed: 10087259 pmcid: 2150572
Schroeder, L. K. et al. Dynamic nanoscale morphology of the ER surveyed by STED microscopy. J. Cell Biol. 218, 83–96 (2019).
pubmed: 30442642 pmcid: 6314542
Baddeley, D. & Bewersdorf, J. Biological insight from super-resolution microscopy: what we can learn from localization-based images. Annu. Rev. Biochem. 87, 965–989 (2018).
pubmed: 29272143
Sigal, Y. M., Zhou, R. & Zhuang, X. Visualizing and discovering cellular structures with super-resolution microscopy. Science 361, 880–887 (2018).
pubmed: 30166485 pmcid: 6535400
von Middendorff, C., Egner, A., Geisler, C., Hell, S. W. & Schonle, A. Isotropic 3D nanoscopy based on single emitter switching. Opt. Express 16, 20774–20788 (2008).
Shtengel, G. et al. Interferometric fluorescent super-resolution microscopy resolves 3D cellular ultrastructure. Proc. Natl Acad. Sci. USA 106, 3125–3130 (2009).
pubmed: 19202073
Aquino, D. et al. Two-color nanoscopy of three-dimensional volumes by 4Pi detection of stochastically switched fluorophores. Nat. Methods 8, 353–359 (2011).
pubmed: 21399636
Huang, F. et al. Ultra-high resolution 3D imaging of whole cells. Cell 166, 1028–1040 (2016).
pubmed: 27397506 pmcid: 5005454
Van Engelenburg, S. B. et al. Distribution of ESCRT machinery at HIV assembly sites reveals virus scaffolding of ESCRT subunits. Science 343, 653–656 (2014).
pubmed: 24436186 pmcid: 4791044
Buttler, C. A. et al. Single molecule fate of HIV-1 envelope reveals late-stage viral lattice incorporation. Nat. Commun. 9, 1861 (2018).
pubmed: 29748537 pmcid: 5945595
Carlini, L., Holden, S. J., Douglass, K. M. & Manley, S. Correction of a depth-dependent lateral distortion in 3D super-resolution imaging. PLoS One 10, e0142949 (2015).
pubmed: 26600467 pmcid: 4658163
Li, Y. M., Wu, Y. L., Hoess, P., Mund, M. & Ries, J. Depth-dependent PSF calibration and aberration correction for 3D single-molecule localization. Biomed. Opt. Express 10, 2708–2718 (2019).
pubmed: 31259045 pmcid: 6583355
Burke, D., Patton, B., Huang, F., Bewersdorf, J. & Booth, M. J. Adaptive optics correction of specimen-induced aberrations in single-molecule switching microscopy. Optica 2, 177–185 (2015).
Schonle, A. & Hell, S. W. Fluorescence nanoscopy goes multicolor. Nat. Biotechnol. 25, 1234–1235 (2007).
pubmed: 17989684
Bossi, M. et al. Multicolor far-field fluorescence nanoscopy through isolated detection of distinct molecular species. Nano Lett. 8, 2463–2468 (2008).
pubmed: 18642961
Baddeley, D. et al. 4D super-resolution microscopy with conventional fluorophores and single wavelength excitation in optically thick cells and tissues. PLoS One 6, e20645 (2011).
pubmed: 21655189 pmcid: 3105105
Lampe, A., Haucke, V., Sigrist, S. J., Heilemann, M. & Schmoranzer, J. Multi-colour direct STORM with red emitting carbocyanines. Biol. Cell 104, 229–237 (2012).
pubmed: 22187967
Zhang, Z., Kenny, S. J., Hauser, M., Li, W. & Xu, K. Ultrahigh-throughput single-molecule spectroscopy and spectrally resolved super-resolution microscopy. Nat. Methods 12, 935–938 (2015).
pubmed: 26280329
Mlodzianoski, M. J., Curthoys, N. M., Gunewardene, M. S., Carter, S. & Hess, S. T. Super-resolution imaging of molecular emission spectra and single molecule spectral fluctuations. PLoS One 11, e0147506 (2016).
pubmed: 27002724 pmcid: 4803349
Dempsey, G. T., Vaughan, J. C., Chen, K. H., Bates, M. & Zhuang, X. Evaluation of fluorophores for optimal performance in localization-based super-resolution imaging. Nat. Methods 8, 1027–1036 (2011).
pubmed: 22056676 pmcid: 3272503
Nieuwenhuizen, R. P. et al. Measuring image resolution in optical nanoscopy. Nat. Methods 10, 557–562 (2013).
pubmed: 23624665 pmcid: 4149789
Ries, J., Kaplan, C., Platonova, E., Eghlidi, H. & Ewers, H. A simple, versatile method for GFP-based super-resolution microscopy via nanobodies. Nat. Methods 9, 582–584 (2012).
pubmed: 22543348
Szymborska, A. et al. Nuclear pore scaffold structure analyzed by super-resolution microscopy and particle averaging. Science 341, 655–658 (2013).
pubmed: 23845946
Schucker, K., Holm, T., Franke, C., Sauer, M. & Benavente, R. Elucidation of synaptonemal complex organization by super-resolution imaging with isotropic resolution. Proc. Natl Acad. Sci. USA 112, 2029–2033 (2015).
pubmed: 25646409
Schmitt, J. et al. Transmembrane protein Sun2 is involved in tethering mammalian meiotic telomeres to the nuclear envelope. Proc. Natl Acad. Sci. USA 104, 7426–7431 (2007).
pubmed: 17452644
Barr, F. A., Puype, M., Vandekerckhove, J. & Warren, G. GRASP65, a protein involved in the stacking of Golgi cisternae. Cell 91, 253–262 (1997).
pubmed: 9346242
Fernandez-Busnadiego, R., Saheki, Y. & De Camilli, P. Three-dimensional architecture of extended synaptotagmin-mediated endoplasmic reticulum–plasma membrane contact sites. Proc. Natl Acad. Sci. USA 112, E2004–E2013 (2015).
pubmed: 25787254
Chung, J. et al. PI4P/phosphatidylserine countertransport at ORP5- and ORP8-mediated ER–plasma membrane contacts. Science 349, 428–432 (2015).
pubmed: 26206935 pmcid: 4638224
Giordano, F. et al. PI(4,5)P
pubmed: 23791178 pmcid: 3716012
Li, X. et al. Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods 10, 584–590 (2013).
pubmed: 23644547 pmcid: 3684049
Wang, Y. et al. Localization events-based sample drift correction for localization microscopy with redundant cross-correlation algorithm. Opt. Express 22, 15982–15991 (2014).
pubmed: 24977854 pmcid: 4162368
Los, G. V. et al. HaloTag: a novel protein labeling technology for cell imaging and protein analysis. ACS Chem. Biol. 3, 373–382 (2008).
pubmed: 18533659
Keppler, A. et al. A general method for the covalent labeling of fusion proteins with small molecules in vivo. Nat. Biotechnol. 21, 86–89 (2003).
pubmed: 12469133
Takakura, H. et al. Long time-lapse nanoscopy with spontaneously blinking membrane probes. Nat. Biotechnol. 35, 773–780 (2017).
pubmed: 28671662 pmcid: 5609855
Douglass, K. M., Sieben, C., Archetti, A., Lambert, A. & Manley, S. Super-resolution imaging of multiple cells by optimised flat-field epi-illumination. Nat. Photonics 10, 705–708 (2016).
pubmed: 27818707 pmcid: 5089541
Deschamps, J., Rowald, A. & Ries, J. Efficient homogeneous illumination and optical sectioning for quantitative single-molecule localization microscopy. Opt. Express 24, 28080–28090 (2016).
pubmed: 27906373
Pallikkuth, S. et al. Sequential super-resolution imaging using DNA strand displacement. PLoS One 13, e0203291 (2018).
pubmed: 30169528 pmcid: 6118358
Jungmann, R. et al. Multiplexed 3D cellular super-resolution imaging with DNA-PAINT and Exchange-PAINT. Nat. Methods 11, 313–318 (2014).
pubmed: 24487583 pmcid: 4153392
Nemoto, Y. & De Camilli, P. Recruitment of an alternatively spliced form of synaptojanin 2 to mitochondria by the interaction with the PDZ domain of a mitochondrial outer membrane protein. EMBO J. 18, 2991–3006 (1999).
pubmed: 10357812 pmcid: 1171381
Huang, F. et al. Video-rate nanoscopy using sCMOS camera-specific single-molecule localization algorithms. Nat. Methods 10, 653–658 (2013).
pubmed: 23708387 pmcid: 3696415
Hanser, B. M., Gustafsson, M. G., Agard, D. A. & Sedat, J. W. Phase-retrieved pupil functions in wide-field fluorescence microscopy. J. Microsc. 216, 32–48 (2004).
pubmed: 15369481
Hoess, P., Mund, M., Reitberger, M. & Ries, J. Dual-color and 3D super-resolution microscopy of multi-protein assemblies. Methods Mol. Biol. 1764, 237–251 (2018).
pubmed: 29605918
Huang, F., Schwartz, S. L., Byars, J. M. & Lidke, K. A. Simultaneous multiple-emitter fitting for single molecule super-resolution imaging. Biomed. Opt. Express 2, 1377–1393 (2011).
pubmed: 21559149 pmcid: 3087594

Auteurs

Yongdeng Zhang (Y)

Department of Cell Biology, Yale School of Medicine, New Haven, CT, USA.

Lena K Schroeder (LK)

Department of Cell Biology, Yale School of Medicine, New Haven, CT, USA.

Mark D Lessard (MD)

Department of Cell Biology, Yale School of Medicine, New Haven, CT, USA.

Phylicia Kidd (P)

Department of Cell Biology, Yale School of Medicine, New Haven, CT, USA.

Jeeyun Chung (J)

Department of Cell Biology, Yale School of Medicine, New Haven, CT, USA.
Department of Neuroscience, Yale School of Medicine, New Haven, CT, USA.
Howard Hughes Medical Institute, Yale School of Medicine, New Haven, CT, USA.

Yuanbin Song (Y)

Section of Hematology, Department of Internal Medicine, Yale School of Medicine, New Haven, CT, USA.

Lorena Benedetti (L)

Department of Cell Biology, Yale School of Medicine, New Haven, CT, USA.
Department of Neuroscience, Yale School of Medicine, New Haven, CT, USA.
Howard Hughes Medical Institute, Yale School of Medicine, New Haven, CT, USA.

Yiming Li (Y)

Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, Heidelberg, Germany.

Jonas Ries (J)

Cell Biology and Biophysics Unit, European Molecular Biology Laboratory, Heidelberg, Germany.

Jonathan B Grimm (JB)

Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA, USA.

Luke D Lavis (LD)

Janelia Research Campus, Howard Hughes Medical Institute, Ashburn, VA, USA.

Pietro De Camilli (P)

Department of Cell Biology, Yale School of Medicine, New Haven, CT, USA.
Department of Neuroscience, Yale School of Medicine, New Haven, CT, USA.
Howard Hughes Medical Institute, Yale School of Medicine, New Haven, CT, USA.
Kavli Institute for Neuroscience, Yale School of Medicine, New Haven, CT, USA.

James E Rothman (JE)

Department of Cell Biology, Yale School of Medicine, New Haven, CT, USA.
Nanobiology Institute, Yale University, West Haven, CT, USA.

David Baddeley (D)

Department of Cell Biology, Yale School of Medicine, New Haven, CT, USA.
Nanobiology Institute, Yale University, West Haven, CT, USA.
Auckland Bioengineering Institute, University of Auckland, Auckland, New Zealand.

Joerg Bewersdorf (J)

Department of Cell Biology, Yale School of Medicine, New Haven, CT, USA. joerg.bewersdorf@yale.edu.
Kavli Institute for Neuroscience, Yale School of Medicine, New Haven, CT, USA. joerg.bewersdorf@yale.edu.
Nanobiology Institute, Yale University, West Haven, CT, USA. joerg.bewersdorf@yale.edu.
Department of Biomedical Engineering, Yale University, New Haven, CT, USA. joerg.bewersdorf@yale.edu.

Articles similaires

[Redispensing of expensive oral anticancer medicines: a practical application].

Lisanne N van Merendonk, Kübra Akgöl, Bastiaan Nuijen
1.00
Humans Antineoplastic Agents Administration, Oral Drug Costs Counterfeit Drugs

Smoking Cessation and Incident Cardiovascular Disease.

Jun Hwan Cho, Seung Yong Shin, Hoseob Kim et al.
1.00
Humans Male Smoking Cessation Cardiovascular Diseases Female
Humans United States Aged Cross-Sectional Studies Medicare Part C
1.00
Humans Yoga Low Back Pain Female Male

Classifications MeSH