scholarly journals Super-Resolution Microscopy Reveals Local Accumulation of Plasma Membrane Gangliosides at Neisseria meningitidis Invasion Sites

2019 ◽  
Vol 7 ◽  
Author(s):  
Jan Schlegel ◽  
Simon Peters ◽  
Sören Doose ◽  
Alexandra Schubert-Unkmeir ◽  
Markus Sauer
Keyword(s):  
Plasma Membrane ◽  
Neisseria Meningitidis ◽  
Super Resolution ◽  
Super Resolution Microscopy ◽  
Local Accumulation

scholarly journals Characterization of Plasma Membrane Ceramides by Super-Resolution Microscopy

2017 ◽  
Vol 56 (22) ◽  
pp. 6131-6135 ◽  
Author(s):  
Anne Burgert ◽  
Jan Schlegel ◽  
Jérôme Bécam ◽  
Sören Doose ◽  
Erhard Bieberich ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Super Resolution ◽  
Super Resolution Microscopy

scholarly journals Direct Observation of Plasma Membrane Domains using Super Resolution Microscopy

2012 ◽  
Vol 102 (3) ◽  
pp. 84a
Author(s):  
Rolf Harkes ◽  
Franziska Zosel ◽  
Anna Pezzarossa ◽  
Thomas Schmidt
Keyword(s):  
Plasma Membrane ◽  
Direct Observation ◽  
Super Resolution ◽  
Membrane Domains ◽  
Plasma Membrane Domains ◽  
Super Resolution Microscopy

scholarly journals Reticulon and CLIMP-63 control nanodomain organization of peripheral ER tubules

2019 ◽  
Author(s):  
Guang Gao ◽  
Chengjia Zhu ◽  
Emma Liu ◽  
Ivan R. Nabi
Keyword(s):  
Endoplasmic Reticulum ◽  
Confocal Microscopy ◽  
High Speed ◽  
Super Resolution ◽  
Live Cell ◽  
Stimulated Emission ◽  
Preferential Segregation ◽  
Stimulated Emission Depletion ◽  
Super Resolution Microscopy ◽  
Local Accumulation

AbstractThe endoplasmic reticulum (ER) is an expansive, membrane-enclosed organelle composed of smooth peripheral tubules and rough, ribosome-studded central ER sheets whose morphology is determined, in part, by the ER-shaping proteins, reticulon and CLIMP-63, respectively. Here, STimulated Emission Depletion (STED) super-resolution microscopy shows that reticulon and CLIMP-63 also control the organization and dynamics of peripheral ER tubule nanodomains. STED imaging shows that lumenal ERmoxGFP, membrane Sec61βGFP, knock-in calreticulin-GFP and antibody-labeled ER resident proteins calnexin and derlin-1 are all localized to periodic puncta along the length of peripheral ER tubules that are not readily observable by diffraction limited confocal microscopy. Reticulon segregates away from and restricts lumenal blob length while CLIMP-63 associates with and increases lumenal blob length. Reticulon and CLIMP-63 also regulate the nanodomain distribution of ER resident proteins, being required for the preferential segregation of calnexin and derlin-1 puncta away from lumenal ERmoxGFP blobs. High-speed (40 ms/frame) live cell STED imaging shows that reticulon and CLIMP-63 control nanoscale compartmentalization of lumenal flow in peripheral ER tubules. Reticulon enhances and CLIMP-63 disrupts the local accumulation of lumenal ERmoxGFP at spatially defined sites along ER tubules. The ER shaping proteins reticulon and CLIMP-63 therefore control lumenal ER nanodomain dynamics, heterogeneity and interaction with ER resident proteins in peripheral ER tubules.

scholarly journals Molecular motion and tridimensional nanoscale localization of kindlin control integrin activation in focal adhesions

2020 ◽  
Author(s):  
Thomas Orré ◽  
Zeynep Karatas ◽  
Birgit Kastberger ◽  
Clément Cabriel ◽  
Ralph T. Böttcher ◽  
...  
Keyword(s):  
Plasma Membrane ◽  
Focal Adhesions ◽  
Super Resolution ◽  
Pleckstrin Homology Domain ◽  
Membrane Diffusion ◽  
Integrin Activation ◽  
Molecular Behavior ◽  
Protein Tracking ◽  
And Function ◽  
Super Resolution Microscopy

AbstractFocal adhesions (FAs) initiate chemical and mechanical signals involved in cell polarity, migration, proliferation and differentiation. Super-resolution microscopy revealed that FAs are organized at the nanoscale into functional layers from the lower plasma membrane to the upper actin cytoskeleton. Yet, how FAs proteins are guided into specific nano-layers to promote interaction with given targets is unknown. Using single protein tracking, super-resolution microscopy and functional assays, we linked the molecular behavior and tridimensional nanoscale localization of kindlin with its function in integrin activation inside FAs. We show that immobilization of integrins in FAs depends on interaction with kindlin. Unlike talin, kindlin displayed free diffusion along the plasma membrane outside and inside FAs. We demonstrate that the kindlin Pleckstrin Homology domain promotes membrane diffusion and localization to the membrane-proximal integrin nano-layer, necessary for kindlin enrichment and function in FAs. Using kindlin-deficient cells, we show that kindlin membrane localization and diffusion are crucial for integrin activation during cell adhesion and spreading. Thus, kindlin uses a different route than talin to reach and activate integrins, providing a possible molecular basis for their complementarity during integrin activation.

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