scholarly journals Polysulfide-triggered fluorescent indicator suitable for super-resolution microscopy and application in imaging

2018 ◽  
Vol 54 (30) ◽  
pp. 3735-3738 ◽  
Author(s):  
Anila Hoskere A. ◽  
Sreejesh Sreedharan ◽  
Firoj Ali ◽  
Carl G. Smythe ◽  
Jim A. Thomas ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Membrane ◽  
Super Resolution ◽  
Molecular Probe ◽  
Fluorescent Indicator ◽  
Super Resolution Microscopy

A new physiologically benign and cell membrane permeable BODIPY based molecular probe, MB-Sn, specifically senses intracellular hydrogen polysulfides (H2Sn, n > 1) localized in the endoplasmic reticulum.

Cubic spline-based depth-dependent localization of mitochondria–endoplasmic reticulum contacts by three-dimensional light-sheet super-resolution microscopy

The Analyst ◽  
2021 ◽  
Author(s):  
Yucheng Sun ◽  
Seungah Lee ◽  
Seong Ho Kang
Keyword(s):  
Endoplasmic Reticulum ◽  
Calcium Homeostasis ◽  
Three Dimensional ◽  
Super Resolution ◽  
Light Sheet ◽  
Cubic Spline ◽  
Contact Distance ◽  
Super Resolution Microscopy

The contact distance between mitochondria (Mito) and endoplasmic reticulum (ER) has received considerable attention owing to their crucial function in maintaining lipid and calcium homeostasis. Herein, cubic spline algorithm-based depth-dependent...

scholarly journals Super Resolution Microscopy and Deep Learning Identify Zika Virus Reorganization of the Endoplasmic Reticulum

2020 ◽  
Author(s):  
Rory K. M. Long ◽  
Kathleen P. Moriarty ◽  
Ben Cardoen ◽  
Guang Gao ◽  
A. Wayne Vogl ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Deep Learning ◽  
Viral Replication ◽  
Zika Virus ◽  
Deep Neural Networks ◽  
Super Resolution ◽  
Zikv Infection ◽  
Subcellular Organelle ◽  
Infected Cells ◽  
Super Resolution Microscopy

AbstractThe endoplasmic reticulum (ER) is a complex subcellular organelle composed of diverse structures such as tubules, sheets and tubular matrices. Flaviviruses such as Zika virus (ZIKV) induce reorganization of endoplasmic reticulum (ER) membranes to facilitate viral replication. Here, using 3D super resolution microscopy, ZIKV infection is shown to induce the formation of dense tubular matrices associated with viral replication in the central ER. Viral non-structural proteins NS4B and NS2B associate with replication complexes within the ZIKV-induced tubular matrix and exhibit distinct ER distributions outside this central ER region. Deep neural networks trained to identify ZIKV-infected versus mock-infected cells successfully identified ZIKV-induced central ER tubular matrices as a determinant of viral infection. Super resolution microscopy and deep learning are therefore able to identify and localize morphological features of the ER and may be of use to screen for inhibitors of infection by ER-reorganizing viruses.

scholarly journals Super resolution microscopy and deep learning identify Zika virus reorganization of the endoplasmic reticulum

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Rory K. M. Long ◽  
Kathleen P. Moriarty ◽  
Ben Cardoen ◽  
Guang Gao ◽  
A. Wayne Vogl ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Deep Learning ◽  
Viral Replication ◽  
Viral Infection ◽  
Zika Virus ◽  
Deep Neural Networks ◽  
Super Resolution ◽  
Zikv Infection ◽  
Infected Cells ◽  
Super Resolution Microscopy

AbstractThe endoplasmic reticulum (ER) is a complex subcellular organelle composed of diverse structures such as tubules, sheets and tubular matrices. Flaviviruses such as Zika virus (ZIKV) induce reorganization of ER membranes to facilitate viral replication. Here, using 3D super resolution microscopy, ZIKV infection is shown to induce the formation of dense tubular matrices associated with viral replication in the central ER. Viral non-structural proteins NS4B and NS2B associate with replication complexes within the ZIKV-induced tubular matrix and exhibit distinct ER distributions outside this central ER region. Deep neural networks trained to distinguish ZIKV-infected versus mock-infected cells successfully identified ZIKV-induced central ER tubular matrices as a determinant of viral infection. Super resolution microscopy and deep learning are therefore able to identify and localize morphological features of the ER and allow for better understanding of how ER morphology changes due to viral infection.

scholarly journals The endoplasmic reticulum adopts two distinct forms of tubules

2021 ◽  
Author(s):  
Ke Xu ◽  
Bowen Wang ◽  
Zhiheng Zhao ◽  
Michael Xiong ◽  
Rui Yan
Keyword(s):  
Endoplasmic Reticulum ◽  
Lipid Synthesis ◽  
Super Resolution ◽  
Cell Types ◽  
Membrane Curvature ◽  
Calcium Storage ◽  
Complex Membrane ◽  
Functional Implications ◽  
Different Cell Types ◽  
Super Resolution Microscopy

Abstract Being the largest and most expansive organelle in the cell, the endoplasmic reticulum (ER) carries diverse key functions from protein and lipid synthesis, protein folding and modification, transport, calcium storage, to organelle interactions1-6. The shaping mechanism of this complex, membrane-bounded organelle is thus of fundamental significance7-21. Using super-resolution microscopy, we uncover the coexistence of two distinct, well-defined forms of ER tubules in the mammalian cell. Whereas an ultrathin form, R1, is consistently covered by the membrane curvature-promoting protein Rtn4, in the second form, R2, Rtn4 curiously appears as two parallel lines at a conserved separation of ~105 nm over long ranges. The two tubule forms together account for ~90% of the total tubule lengths, with either one being dominant in different cell types. The R1-R2 dichotomy and the final tubule geometry are both co-regulated by Rtn4 and the ER sheet-maintaining protein Climp63, which respectively define the edge curvature and lumen height of the R2 tubules to generate a ribbon-like structure of well-defined width. The R1 and R2 tubules undergo active remodeling in the cell as they differently accommodate proteins, with the former effectively excluding ER-luminal proteins and ER-membrane proteins with large intraluminal domains. We thus unveil a dynamic ER-tubule structural dichotomy with intriguing functional implications.

scholarly journals The endoplasmic reticulum adopts two distinct tubule forms

2021 ◽  
Author(s):  
Bowen Wang ◽  
Zhiheng Zhao ◽  
Michael Xiong ◽  
Rui Yan ◽  
Ke Xu
Keyword(s):  
Endoplasmic Reticulum ◽  
Super Resolution ◽  
Cell Types ◽  
Membrane Curvature ◽  
Parallel Lines ◽  
Native Cell ◽  
Functional Implications ◽  
Different Cell Types ◽  
Super Resolution Microscopy ◽  
Er Membrane

The endoplasmic reticulum (ER) is a versatile organelle with diverse functions. Through super-resolution microscopy, we show that the peripheral ER in the mammalian cell adopts two distinct forms of tubules. Whereas an ultrathin form, R1, is consistently covered by ER-membrane curvature-promoting proteins, e.g., Rtn4 in the native cell, in the second form, R2, Rtn4 and analogs are arranged into two parallel lines at a conserved separation of ~105 nm over long ranges. The two tubule forms together account for ~90% of the total tubule length in the cell, with either one being dominant in different cell types. The R1-R2 dichotomy and the final tubule geometry are both co-regulated by Rtn4 (and analogs) and the ER sheet-maintaining protein Climp63, which respectively define the edge curvature and lumen height of the R2 tubules to generate a ribbon-like structure of well-defined width. Accordingly, the R2 tubule width correlates positively with the Climp63 intralumenal size. The R1 and R2 tubules undergo active remodeling at the second/sub-second time scales as they differently accommodate proteins, with the former effectively excluding ER-luminal proteins and ER-membrane proteins with large intraluminal domains. We thus uncover a dynamic structural dichotomy for ER tubules with intriguing functional implications.

scholarly journals New insights into protein secretion: TANGO1 runs rings around the COPII coat

2017 ◽  
Vol 216 (4) ◽  
pp. 859-861 ◽  
Author(s):  
Benjamin S. Glick
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Secretion ◽  
Super Resolution ◽  
Cell Biol ◽  
Er Exit Sites ◽  
Er Export ◽  
Super Resolution Microscopy

In this issue, Liu et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201611088) and Raote et al. (2017. J. Cell Biol. https://doi.org/10.1083/jcb.201608080) use super-resolution microscopy to visualize large COPII-coated endoplasmic reticulum (ER) export carriers. Rings of TANGO1 surround COPII, implicating TANGO1 in organizing ER exit sites and in regulating COPII coat dynamics and geometry.

A molecular probe based on pyrimidine imidazole derivatives for stable super-resolution endoplasmic reticulum imaging in living cells

2018 ◽  
Vol 42 (18) ◽  
pp. 14725-14728 ◽  
Author(s):  
Ling Hu ◽  
Sajid Hussain ◽  
Tianyan Liu ◽  
Yuanzhen Yue ◽  
Jiejie Liu ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Super Resolution ◽  
Living Cells ◽  
Molecular Probes ◽  
Living Systems ◽  
Molecular Probe ◽  
Imidazole Derivatives ◽  
Two Photon Microscopy ◽  
Two Photon

Multi-functional florescent dyes capable of acting as molecular probes in living systems under two-photon microscopy, as well as super-resolution nanoscopy, are of great interest.

Aptamer-recognized carbohydrates on the cell membrane revealed by super-resolution microscopy

Nanoscale ◽  
2018 ◽  
Vol 10 (16) ◽  
pp. 7457-7464 ◽  
Author(s):  
Yingying Jing ◽  
Mingjun Cai ◽  
Haijiao Xu ◽  
Lulu Zhou ◽  
Qiuyan Yan ◽  
...  
Keyword(s):  
Cell Membrane ◽  
Super Resolution ◽  
Nanometer Scale ◽  
Detailed Structure ◽  
Super Resolution Microscopy

By using dSTORM, aptamer-recognized method was compared with lectin-recognized method on visualizing the detailed structure of GalNAc at the nanometer scale.

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.

Super-Resolution Microscopy in Studying the Structure and Function of the Cell Nucleus

Acta Naturae ◽  
2017 ◽  
Vol 9 (4) ◽  
pp. 42-51
Author(s):  
S. S. Ryabichko ◽  
◽  
A. N. Ibragimov ◽  
L. A. Lebedeva ◽  
E. N. Kozlov ◽  
...  
Keyword(s):  
Cell Nucleus ◽  
Super Resolution ◽  
Structure And Function ◽  
And Function ◽  
Super Resolution Microscopy
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