Integrated electron microscopy: super-duper resolution.
Since its inception, electron microscopy (EM) has revealed that cellular membranes are organized into structurally distinct subdomains, created by localized protein and lipid assemblies to perform specific complex cellular functions. Caveolae are membrane subdomains that function as signaling platfo...
| Main Authors: | , |
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| Format: | Article |
| Language: | English |
| Published: |
Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS Biology |
| Online Access: | http://europepmc.org/articles/PMC3754885?pdf=render |
| _version_ | 1818398229158428672 |
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| author | Jacomine Krijnse Locker Sandra L Schmid |
| author_facet | Jacomine Krijnse Locker Sandra L Schmid |
| author_sort | Jacomine Krijnse Locker |
| collection | DOAJ |
| description | Since its inception, electron microscopy (EM) has revealed that cellular membranes are organized into structurally distinct subdomains, created by localized protein and lipid assemblies to perform specific complex cellular functions. Caveolae are membrane subdomains that function as signaling platforms, endocytic carriers, sensors of membrane tension, and mechanical stress, as well as in lipid homeostasis. They were first discovered almost 60 years ago by pioneering electron microscopists. While new and exciting developments in SUPER-resolution fluorescent light microscopy facilitate studies of the spatial organization of fluorescently labeled protein components, these techniques cannot reveal the underlying cellular structures. Thus, equally exciting are developments in EM: genetically encoded probes for protein localization at sub-10 nm resolution, more powerful instruments that allow imaging of larger cell volumes, and computational methods for reconstructing three-dimensional images. Used in combination, as done by Ludwig et al. in the current issue of PLOS Biology, these tools reveal high-resolution insights into the composition and organization of the caveolae coat and the formation of these specialized structures. Together, these advances are contributing to a resurgence in EM. |
| first_indexed | 2024-12-14T07:01:28Z |
| format | Article |
| id | doaj.art-ff54030ec6f04c5fa96f599f11c11f03 |
| institution | Directory Open Access Journal |
| issn | 1544-9173 1545-7885 |
| language | English |
| last_indexed | 2024-12-14T07:01:28Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS Biology |
| spelling | doaj.art-ff54030ec6f04c5fa96f599f11c11f032022-12-21T23:12:24ZengPublic Library of Science (PLoS)PLoS Biology1544-91731545-78852013-01-01118e100163910.1371/journal.pbio.1001639Integrated electron microscopy: super-duper resolution.Jacomine Krijnse LockerSandra L SchmidSince its inception, electron microscopy (EM) has revealed that cellular membranes are organized into structurally distinct subdomains, created by localized protein and lipid assemblies to perform specific complex cellular functions. Caveolae are membrane subdomains that function as signaling platforms, endocytic carriers, sensors of membrane tension, and mechanical stress, as well as in lipid homeostasis. They were first discovered almost 60 years ago by pioneering electron microscopists. While new and exciting developments in SUPER-resolution fluorescent light microscopy facilitate studies of the spatial organization of fluorescently labeled protein components, these techniques cannot reveal the underlying cellular structures. Thus, equally exciting are developments in EM: genetically encoded probes for protein localization at sub-10 nm resolution, more powerful instruments that allow imaging of larger cell volumes, and computational methods for reconstructing three-dimensional images. Used in combination, as done by Ludwig et al. in the current issue of PLOS Biology, these tools reveal high-resolution insights into the composition and organization of the caveolae coat and the formation of these specialized structures. Together, these advances are contributing to a resurgence in EM.http://europepmc.org/articles/PMC3754885?pdf=render |
| spellingShingle | Jacomine Krijnse Locker Sandra L Schmid Integrated electron microscopy: super-duper resolution. PLoS Biology |
| title | Integrated electron microscopy: super-duper resolution. |
| title_full | Integrated electron microscopy: super-duper resolution. |
| title_fullStr | Integrated electron microscopy: super-duper resolution. |
| title_full_unstemmed | Integrated electron microscopy: super-duper resolution. |
| title_short | Integrated electron microscopy: super-duper resolution. |
| title_sort | integrated electron microscopy super duper resolution |
| url | http://europepmc.org/articles/PMC3754885?pdf=render |
| work_keys_str_mv | AT jacominekrijnselocker integratedelectronmicroscopysuperduperresolution AT sandralschmid integratedelectronmicroscopysuperduperresolution |