Erratum: Super-resolution mapping of glutamate receptors in C. Elegans by confocal correlated PALM (Scientific Reports (2016) 5 (13532) DOI: 10.1038/srep13532);Super-resolution mapping of glutamate receptors in C. elegans by confocal correlated PALM

Scientific Reports

Volumn 5, Issue , 2015, Pages

  Vangindertael, Jeroen ^a,b   Beets, Isabel ^b   Rocha, Susana ^a,b   Dedecker, Peter ^a   Schoofs, Liliane ^b   Vanhoorelbeeke, Karen ^b   Hofkens, Johan ^a,c   Mizuno, Hideaki ^b  

^a Katholieke Universiteit Leuven   (Belgium)

^b UNIVERSITY OF LEUVEN   (Belgium)

^c UNIVERSITY OF COPENHAGEN   (Denmark)

Author keywords

[No Author keywords available]

Indexed keywords

AMPA RECEPTOR; CAENORHABDITIS ELEGANS PROTEIN; GLR-1 PROTEIN, C ELEGANS; PHOTOPROTEIN;

ANIMAL; CAENORHABDITIS ELEGANS; CLUSTER ANALYSIS; CONFOCAL MICROSCOPY; FLUORESCENCE MICROSCOPY; GENETICS; METABOLISM; NERVE CELL; PATHOLOGY; PLASMID; PROCEDURES; TRANSGENIC ANIMAL;

ANIMALS; ANIMALS, GENETICALLY MODIFIED; CAENORHABDITIS ELEGANS; CAENORHABDITIS ELEGANS PROTEINS; CLUSTER ANALYSIS; LUMINESCENT PROTEINS; MICROSCOPY, CONFOCAL; MICROSCOPY, FLUORESCENCE; NEURONS; PLASMIDS; RECEPTORS, AMPA;

EID: 84940867461     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep26047     Document Type: Erratum

References (65)

1. Betzig, E. et al. Imaging Intracellular Fluorescent Proteins at Nanometer Resolution. Science 313, 1642-1645 (2006).
2. Hess, S. T., Girirajan, T. P. K. & Mason, M. D. Ultra-High Resolution Imaging by Fluorescence Photoactivation Localization Microscopy. Biophys J 91, 4258-4272 (2006).
3. Rust, M. J., Bates, M. & Zhuang, X. Sub-diffraction-limit imaging by stochastic optical reconstruction microscopy (STORM). Nat Meth 3, 793-796 (2006).
4. Hell, S. W. & Wichmann, J. Breaking the diffraction resolution limit by stimulated emission: stimulated-emission-depletion fluorescence microscopy. Opt. Lett. 19, 780-782 (1994).
5. Gustafsson, M. G. L. Surpassing the lateral resolution limit by a factor of two using structured illumination microscopy. J Microsc 198, 82-87 (2000).
6. Dertinger, T., Colyer, R., Iyer, G., Weiss, S. & Enderlein, J. Fast, background-free, 3D super-resolution optical fluctuation imaging (SOFI). Proc Natl Acad Sci USA 106, 22287-22292 (2009).
7. Heilemann, M. et al. Subdiffraction-Resolution Fluorescence Imaging with Conventional Fluorescent Probes. Angew Chem Int Ed Engl 47, 6172-6176 (2008).
8. Dedecker, P., Mo, G. C. H., Dertinger, T. & Zhang, J. Widely accessible method for superresolution fluorescence imaging of living systems. Proc Natl Acad Sci USA 109, 10909-10914 (2012).
9. Roeffaers, M. B. J. et al. Super-Resolution Reactivity Mapping of Nanostructured Catalyst Particles. Angew Chem Int Ed Engl 48, 9285-9289 (2009).
10. Flors, C. et al. A Stroboscopic Approach for Fast Photoactivation? Localization Microscopy with Dronpa Mutants. J Am Chem Soc 129, 13970-13977 (2007).
11. McKinney, S. A., Murphy, C. S., Hazelwood, K. L., Davidson, M. W. & Looger, L. L. A bright and photostable photoconvertible fluorescent protein. Nat Meth 6, 131-133 (2009).
12. Annibale, P., Scarselli, M., Kodiyan, A. & Radenovic, A. Photoactivatable Fluorescent Protein mEos2 Displays Repeated Photoactivation after a Long-Lived Dark State in the Red Photoconverted Form. J Phys Chem Lett 1, 1506-1510 (2010).
13. Schmidt, T., Schütz, G. J., Baumgartner, W., Gruber, H. J. & Schindler, H. Imaging of single molecule diffusion. Proc Natl Acad Sci USA 93, 2926-2929 (1996).
14. Berning, S., Willig, K. I., Steffens, H., Dibaj, P. & Hell, S. W. Nanoscopy in a Living Mouse Brain. Science 335, 551 (2012).
15. York, A. G. et al. Resolution doubling in live, multicellular organisms via multifocal structured illumination microscopy. Nat Meth 9, 749-754 (2012).
16. Gao, L. et al. Noninvasive Imaging beyond the Diffraction Limit of 3D Dynamics in Thickly Fluorescent Specimens. Cell 151, 1370-1385 (2012).
17. Willig, Katrin I. et al. Nanoscopy of Filamentous Actin in Cortical Dendrites of a Living Mouse. Biophys J 106, L01-L03 (2014).
18. Rankin, B. R. et al. Nanoscopy in a Living Multicellular Organism Expressing GFP. Biophys J 100, L63-L65 (2011).
19. Axelrod, D. Total internal reflection fluorescence microscopy. Methods Cell Biol 30, 245-270 (1989).
20. Robin, F. B., McFadden, W. M., Yao, B. & Munro, E. M. Single-molecule analysis of cell surface dynamics in Caenorhabditis elegans embryos. Nat Meth 11, 677-682 (2014).
21. White, J. G., Southgate, E., Thomson, J. N. & Brenner, S. The Structure of the Nervous System of the Nematode Caenorhabditis elegans. Philos Trans R Soc Lond, B, Biol Sci 314, 1-340 (1986).
22. Bargmann, C. I. Neurobiology of the Caenorhabditis elegans Genome. Science 282, 2028-2033 (1998).
23. Brockie, P. J. & Maricq, A. V. Ionotropic Glutamate Receptors in Caenorhabditis elegans. Neurosignals 12, 108-125 (2003).
24. Maricq, A. V., Peckol, E., Driscoll, M. & Bargmann, C. I. Mechanosensory signalling in C. elegans mediated by the GLR-1 glutamate receptor. Nature 378, 78-81 (1995).
25. Hart, A. C., Sims, S. & Kaplan, J. M. Synaptic code for sensory modalities revealed by C. elegans GLR-1 glutamate receptor. Nature 378, 82-85 (1995).
26. Rongo, C., Whitfield, C. W., Rodal, A., Kim, S. K. & Kaplan, J. M. LIN-10 Is a Shared Component of the Polarized Protein Localization Pathways in Neurons and Epithelia. Cell 94, 751-759 (1998).
27. Burbea, M., Dreier, L., Dittman, J. S., Grunwald, M. E. & Kaplan, J. M. Ubiquitin and AP180 Regulate the Abundance of GLR-1 Glutamate Receptors at Postsynaptic Elements in C. elegans. Neuron 35, 107-120 (2002).
28. Rose, J. K., Kaun, K. R., Chen, S. H. & Rankin, C. H. GLR-1, a Non-NMDA Glutamate Receptor Homolog, Is Critical for Long-Term Memory in Caenorhabditis elegans. J Neurosci 23, 9595-9599 (2003).
29. Rankin, C. H., Beck, C. D. O. & Chiba, C. M. Caenorhabditis elegans: A new model system for the study of learning and memory. Behav Brain Res 37, 89-92 (1990).
30. Hadziselimovic, N. et al. Forgetting Is Regulated via Musashi-Mediated Translational Control of the Arp2/3 Complex. Cell 156, 1153-1166 (2014).
31. Altun, Z. Individual Neurons. In WormAtlas (2015) Available at: http://www.wormatlas.org/neurons/IndividualNeurons/Neuronframeset.html (Accessed: 9th June 2015).
32. Chang, H. C.-H. & Rongo, C. Cytosolic tail sequences and subunit interactions are critical for synaptic localization of glutamate receptors. J Cell Sci 118, 1945-1956 (2005).
33. Brockie, P. J., Madsen, D. M., Zheng, Y., Mellem, J. & Maricq, A. V. Differential Expression of Glutamate Receptor Subunits in the Nervous System of Caenorhabditis elegans and Their Regulation by the Homeodomain Protein UNC-42. J Neurosci 21, 1510-1522 (2001).
34. Choi, W. et al. Tomographic phase microscopy. Nat Meth 4, 717-719 (2007).
35. Hell, S., Reiner, G., Cremer, C. & Stelzer, E. H. K. Aberrations in confocal fluorescence microscopy induced by mismatches in refractive index. J Microsc 169, 391-405 (1993).
36. Tokunaga, M., Imamoto, N. & Sakata-Sogawa, K. Highly inclined thin illumination enables clear single-molecule imaging in cells. Nat Meth 5, 159-161 (2008).
37. Dedecker, P., Duwé, S., Neely, R. K. & Zhang, J. Localizer: fast, accurate, open-source, and modular software package for superresolution microscopy. J Biomed Opt 17, 126008-126008 (2012).
38. Annibale, P., Vanni, S., Scarselli, M., Rothlisberger, U. & Radenovic, A. Identification of clustering artifacts in photoactivated localization microscopy. Nat Meth 8, 527-528 (2011).
39. Annibale, P., Vanni, S., Scarselli, M., Rothlisberger, U. & Radenovic, A. Quantitative Photo Activated Localization Microscopy: Unraveling the Effects of Photoblinking. PLoS ONE 6, e22678 (2011).
40. Ribrault, C., Sekimoto, K. & Triller, A. From the stochasticity of molecular processes to the variability of synaptic transmission. Nat Rev Neurosci 12, 375-387 (2011).
41. Ripley, B. D. Modelling Spatial Patterns. J Roy Stat Soc B Met 39, 172-212 (1977).
42. Sengupta, P. & Lippincott-Schwartz, J. Quantitative analysis of photoactivated localization microscopy (PALM) datasets using pair-correlation analysis. Bioessays 34, 396-405 (2012).
43. Nair, D. et al. Super-Resolution Imaging Reveals That AMPA Receptors Inside Synapses Are Dynamically Organized in Nanodomains Regulated by PSD95. J Neurosci 33, 13204-13224 (2013).
44. Cox, G. Biological confocal microscopy. Mater Today 5, 34-41 (2002).
45. Friedrich, M. et al. Detection of single quantum dots in model organisms with sheet illumination microscopy. Biochem Biophys Res Commun 390, 722-727 (2009).
46. Hoerndli, Frédéric J. et al. Kinesin-1 Regulates Synaptic Strength by Mediating the Delivery, Removal, and Redistribution of AMPA Receptors. Neuron 80, 1421-1437 (2013).
47. Rongo, C. & Kaplan, J. M. CaMKII regulates the density of central glutamatergic synapses in vivo. Nature 402, 195-199 (1999).
48. Rongo, C. Going Mobile: AMPA receptors move synapse to synapse in vivo. Neuron 80, 1339-1341 (2013).
49. MacGillavry, H. D., Song, Y., Raghavachari, S. & Blanpied, T. A. Nanoscale Scaffolding Domains within the Postsynaptic Density Concentrate Synaptic AMPA Receptors. Neuron 78, 615-622 (2013).
50. Dani, A., Huang, B., Bergan, J., Dulac, C. & Zhuang, X. Superresolution Imaging of Chemical Synapses in the Brain. Neuron 68, 843-856 (2010).
51. Takamori, S. et al. Molecular Anatomy of a Trafficking Organelle. Cell 127, 831-846 (2006).
52. Booth, M. J., Neil, M. A. A., Ju͉kaitis, R. & Wilson, T. Adaptive aberration correction in a confocal microscope. Proc Natl Acad Sci USA 99, 5788-5792 (2002).
53. Ji, N., Milkie, D. E. & Betzig, E. Adaptive optics via pupil segmentation for high-resolution imaging in biological tissues. Nat Meth 7, 141-147 (2010).
54. Ji, N., Sato, T. R. & Betzig, E. Characterization and adaptive optical correction of aberrations during in vivo imaging in the mouse cortex. Proc Natl Acad Sci USA 109, 22-27 (2012).
55. Shtengel, G. et al. Interferometric fluorescent super-resolution microscopy resolves 3D cellular ultrastructure. Proc Natl Acad Sci USA 106, 3125-3130 (2009).
56. Huang, B., Wang, W., Bates, M. & Zhuang, X. Three-Dimensional Super-Resolution Imaging by Stochastic Optical Reconstruction Microscopy. Science 319, 810-813 (2008).
57. Juette, M. F. et al. Three-dimensional sub-100 nm resolution fluorescence microscopy of thick samples. Nat Meth 5, 527-529 (2008).
58. Pavani, S. R. P. et al. Three-dimensional, single-molecule fluorescence imaging beyond the diffraction limit by using a doublehelix point spread function. Proc Natl Acad Sci USA 106, 2995-2999 (2009).
59. Huisken, J., Swoger, J., Del Bene, F., Wittbrodt, J. & Stelzer, E. H. K. Optical Sectioning Deep Inside Live Embryos by Selective Plane Illumination Microscopy. Science 305, 1007-1009 (2004).
60. Brenner, S. THE GENETICS OF CAENORHABDITIS ELEGANS. Genetics 77, 71-94 (1974).
61. Mello, C. C., Kramer, J. M., Stinchcomb, D. & Ambros, V. Efficient gene transfer in C.elegans: extrachromosomal maintenance and integration of transforming sequences. EMBO J 10, 3959-3970 (1991).
62. Stiernagle, T. Maintenance of C. elegans. (WormBook, ed. The C. elegans Research Community, 2006).
63. Tanaka, K. A. K. et al. Membrane molecules mobile even after chemical fixation. Nat Meth 7, 865-866 (2010).
64. Mlodzianoski, M. J. et al. Sample drift correction in 3D fluorescence photoactivation localization microscopy. Opt Express 19, 15009-15019 (2011).
65. Prescher, J. et al. Super-Resolution Imaging of ESCRT-Proteins at HIV-1 Assembly Sites. PLoS Pathog 11, e1004677 (2015).