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Proteomes 2016, 4(4), 36; doi:10.3390/proteomes4040036

Let There Be Light!

1
Department of Pharmaceutical Biosciences, Pharmaceutical Cell Biology, Biomedical Center, Box 594, Uppsala University, SE-751 08 Uppsala, Sweden
2
Department of Systemic Cell Biology, Max Planck Institute of Molecular Physiology, Otto-Hahn-Straße 11, 44227 Dortmund, Germany
3
Department of Immunology, Genetics and Pathology, Dag Hamarskjölds väg 14B, Rudbeck Laboratory, Uppsala University, 751 85 Uppsala, Sweden
4
Faculty of Chemistry and Chemical Biology, Technical University of Dortmund, Otto-Hahn-Straße 6, 44221 Dortmund, Germany
5
Department of Chemistry-BMC, Box 576, Uppsala University, SE-751 23 Uppsala, Sweden
*
Author to whom correspondence should be addressed.
Academic Editors: Jens R. Coorssen, Alfred L. Yergey and Jacek R. Wisniewski
Received: 17 October 2016 / Revised: 15 November 2016 / Accepted: 23 November 2016 / Published: 29 November 2016
View Full-Text   |   Download PDF [5670 KB, uploaded 29 November 2016]   |  

Abstract

The invention of the microscope has been fundamental for the understanding of tissue architecture and subcellular structures. With the advancement of higher magnification microscopes came the development of various molecular biology tools such as Förster resonance energy transfer (FRET) and in situ proximity ligation assay (in situ PLA) to monitor protein interactions. Microscopy has become a commonly used method for the investigation of molecular events within the cell, for the identification of key players in signaling networks, and the activation of these pathways. Multiple approaches are available for functional analyses in single cells. They provide information not only on the localization of proteins at a given time point, but also on their expression levels and activity states, allowing us to pinpoint hallmarks of different cellular identities within tissues in health and disease. Clever solutions to increase the sensitivity of molecular tools, the possibilities for multiplexing, as well as image resolution have recently been introduced; however, these methods have their pros and cons. Therefore, one needs to carefully consider the biological question of interest along with the nature of the sample before choosing the most suitable method or combination of methods. Herein, we review a few of the most exciting microscopy-based molecular techniques for proteomic analysis and cover the benefits as well as the disadvantages of their use. View Full-Text
Keywords: high resolution microscopy; protein–protein interactions; post-translational modifications; FRET; in situ PLA; proxHCR high resolution microscopy; protein–protein interactions; post-translational modifications; FRET; in situ PLA; proxHCR
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This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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Raykova, D.; Koos, B.; Asplund, A.; Gelléri, M.; Ivarsson, Y.; Danielson, U.H.; Söderberg, O. Let There Be Light! Proteomes 2016, 4, 36.

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