The tetraspanin web revisited by super-resolution microscopy

The spatial organization of membrane proteins in the plasma membrane is critical for signal transduction, cell communication and membrane trafficking. Tetraspanins organize functional higher-order protein complexes called ‘tetraspanin-enriched microdomains (TEMs)’ via interactions with partner molec...

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Main Authors:	Zuidscherwoude, Malou, Göttfert, Fabian, Dunlock, Vera Marie E., Figdor, Carl G., van den Bogaart, Geert, Spriel, Annemiek B. van
Format:	Online
Language:	English
Published:	Nature Publishing Group 2015
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4505338/

id	pubmed-4505338
recordtype	oai_dc
spelling	pubmed-45053382015-07-23 The tetraspanin web revisited by super-resolution microscopy Zuidscherwoude, Malou Göttfert, Fabian Dunlock, Vera Marie E. Figdor, Carl G. van den Bogaart, Geert Spriel, Annemiek B. van Article The spatial organization of membrane proteins in the plasma membrane is critical for signal transduction, cell communication and membrane trafficking. Tetraspanins organize functional higher-order protein complexes called ‘tetraspanin-enriched microdomains (TEMs)’ via interactions with partner molecules and other tetraspanins. Still, the nanoscale organization of TEMs in native plasma membranes has not been resolved. Here, we elucidated the size, density and distribution of TEMs in the plasma membrane of human B cells and dendritic cells using dual color stimulated emission depletion (STED) microscopy. We demonstrate that tetraspanins form individual nanoclusters smaller than 120 nm and quantified that a single tetraspanin CD53 cluster contains less than ten CD53 molecules. CD53 and CD37 domains were adjacent to and displayed only minor overlap with clusters containing tetraspanins CD81 or CD82. Moreover, CD53 and CD81 were found in closer proximity to their partners MHC class II and CD19 than to other tetraspanins. Although these results indicate that tetraspanin domains are adjacently positioned in the plasma membrane, they challenge the current view of the tetraspanin web of multiple tetraspanin species organized into a single domain. This study increases the molecular understanding of TEMs at the nanoscale level which is essential for comprehending tetraspanin function in cell biology. Nature Publishing Group 2015-07-17 /pmc/articles/PMC4505338/ /pubmed/26183063 http://dx.doi.org/10.1038/srep12201 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Zuidscherwoude, Malou Göttfert, Fabian Dunlock, Vera Marie E. Figdor, Carl G. van den Bogaart, Geert Spriel, Annemiek B. van
spellingShingle	Zuidscherwoude, Malou Göttfert, Fabian Dunlock, Vera Marie E. Figdor, Carl G. van den Bogaart, Geert Spriel, Annemiek B. van The tetraspanin web revisited by super-resolution microscopy
author_facet	Zuidscherwoude, Malou Göttfert, Fabian Dunlock, Vera Marie E. Figdor, Carl G. van den Bogaart, Geert Spriel, Annemiek B. van
author_sort	Zuidscherwoude, Malou
title	The tetraspanin web revisited by super-resolution microscopy
title_short	The tetraspanin web revisited by super-resolution microscopy
title_full	The tetraspanin web revisited by super-resolution microscopy
title_fullStr	The tetraspanin web revisited by super-resolution microscopy
title_full_unstemmed	The tetraspanin web revisited by super-resolution microscopy
title_sort	tetraspanin web revisited by super-resolution microscopy
description	The spatial organization of membrane proteins in the plasma membrane is critical for signal transduction, cell communication and membrane trafficking. Tetraspanins organize functional higher-order protein complexes called ‘tetraspanin-enriched microdomains (TEMs)’ via interactions with partner molecules and other tetraspanins. Still, the nanoscale organization of TEMs in native plasma membranes has not been resolved. Here, we elucidated the size, density and distribution of TEMs in the plasma membrane of human B cells and dendritic cells using dual color stimulated emission depletion (STED) microscopy. We demonstrate that tetraspanins form individual nanoclusters smaller than 120 nm and quantified that a single tetraspanin CD53 cluster contains less than ten CD53 molecules. CD53 and CD37 domains were adjacent to and displayed only minor overlap with clusters containing tetraspanins CD81 or CD82. Moreover, CD53 and CD81 were found in closer proximity to their partners MHC class II and CD19 than to other tetraspanins. Although these results indicate that tetraspanin domains are adjacently positioned in the plasma membrane, they challenge the current view of the tetraspanin web of multiple tetraspanin species organized into a single domain. This study increases the molecular understanding of TEMs at the nanoscale level which is essential for comprehending tetraspanin function in cell biology.
publisher	Nature Publishing Group
publishDate	2015
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4505338/
_version_	1613248887780278272

The tetraspanin web revisited by super-resolution microscopy

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