scholarly journals Endoplasmic reticulum–associated degradation regulates mitochondrial dynamics in brown adipocytes

Science ◽  
2020 ◽  
Vol 368 (6486) ◽  
pp. 54-60 ◽  
Author(s):  
Zhangsen Zhou ◽  
Mauricio Torres ◽  
Haibo Sha ◽  
Christopher J. Halbrook ◽  
Françoise Van den Bergh ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Mitochondrial Dynamics ◽  
Three Dimensional ◽  
Sigma Receptor ◽  
High Resolution Imaging ◽  
Brown Adipocytes ◽  
Physiological Importance ◽  
Endoplasmic Reticulum Associated Degradation ◽  
Cold Sensitive ◽  
Resolution Imaging

The endoplasmic reticulum (ER) engages mitochondria at specialized ER domains known as mitochondria-associated membranes (MAMs). Here, we used three-dimensional high-resolution imaging to investigate the formation of pleomorphic “megamitochondria” with altered MAMs in brown adipocytes lacking the Sel1L-Hrd1 protein complex of ER-associated protein degradation (ERAD). Mice with ERAD deficiency in brown adipocytes were cold sensitive and exhibited mitochondrial dysfunction. ERAD deficiency affected ER-mitochondria contacts and mitochondrial dynamics, at least in part, by regulating the turnover of the MAM protein, sigma receptor 1 (SigmaR1). Thus, our study provides molecular insights into ER-mitochondrial cross-talk and expands our understanding of the physiological importance of Sel1L-Hrd1 ERAD.

scholarly journals Plastic embedding immunolabeled large-volume samples for three-dimensional high-resolution imaging

2017 ◽  
Vol 8 (8) ◽  
pp. 3583 ◽  
Author(s):  
Yadong Gang ◽  
Xiuli Liu ◽  
Xiaojun Wang ◽  
Qi Zhang ◽  
Hongfu Zhou ◽  
...  
Keyword(s):  
High Resolution ◽  
Large Volume ◽  
Three Dimensional ◽  
High Resolution Imaging ◽  
Plastic Embedding ◽  
Resolution Imaging

scholarly journals Three-Dimensional High-Resolution Imaging of Gold Nanorods Uptake in Sentinel Lymph Nodes

Nano Letters ◽  
2011 ◽  
Vol 11 (7) ◽  
pp. 2938-2943 ◽  
Author(s):  
Yeongri Jung ◽  
Roberto Reif ◽  
Yaguang Zeng ◽  
Ruikang K. Wang
Keyword(s):  
High Resolution ◽  
Lymph Nodes ◽  
Gold Nanorods ◽  
Three Dimensional ◽  
Sentinel Lymph Nodes ◽  
High Resolution Imaging ◽  
Resolution Imaging

In Vivo Three-Dimensional High-Resolution Imaging of Rodent Retina with Spectral-Domain Optical Coherence Tomography

2007 ◽  
Vol 48 (4) ◽  
pp. 1808 ◽  
Author(s):  
Marco Ruggeri ◽  
Hassan Wehbe ◽  
Shuliang Jiao ◽  
Giovanni Gregori ◽  
Maria E. Jockovich ◽  
...  
Keyword(s):  
Optical Coherence Tomography ◽  
High Resolution ◽  
Three Dimensional ◽  
Spectral Domain ◽  
High Resolution Imaging ◽  
Optical Coherence ◽  
Resolution Imaging

scholarly journals mDia1/3-dependent actin polymerization spatiotemporally controls LAT phosphorylation by Zap70 at the immune synapse

2020 ◽  
Vol 6 (1) ◽  
pp. eaay2432 ◽  
Author(s):  
D. Thumkeo ◽  
Y. Katsura ◽  
Y. Nishimura ◽  
P. Kanchanawong ◽  
K. Tohyama ◽  
...  
Keyword(s):  
Actin Polymerization ◽  
Transmembrane Protein ◽  
Three Dimensional ◽  
Cell Receptor ◽  
Filamentous Actin ◽  
Tcr Signaling ◽  
Immune Synapse ◽  
Physiological Importance ◽  
Resolution Imaging ◽  
Tcr Activation

The mechanism by which the cytosolic protein Zap70 physically interacts with and phosphorylates its substrate, the transmembrane protein LAT, upon T cell receptor (TCR) stimulation remains largely obscure. In this study, we found that the pharmacological inhibition of formins, a major class of actin nucleators, suppressed LAT phosphorylation by Zap70, despite TCR stimulation–dependent phosphorylation of Zap70 remaining intact. High-resolution imaging and three-dimensional image reconstruction revealed that localization of phosphorylated Zap70 to the immune synapse (IS) and subsequent LAT phosphorylation are critically dependent on formin-mediated actin polymerization. Using knockout mice, we identify mDia1 and mDia3, which are highly expressed in T cells and which localize to the IS upon TCR activation, as the critical formins mediating this process. Our findings therefore describe previously unsuspected roles for mDia1 and mDia3 in the spatiotemporal control of Zap70-dependent LAT phosphorylation at the IS through regulation of filamentous actin, and underscore their physiological importance in TCR signaling.

scholarly journals Three-dimensional imaging of mitochondrial cristae complexity using cryo-soft X-ray tomography

2020 ◽  
Vol 10 (1) ◽  
Author(s):  
Carla C. Polo ◽  
Miriam H. Fonseca-Alaniz ◽  
Jian-Hua Chen ◽  
Axel Ekman ◽  
Gerry McDermott ◽  
...  
Keyword(s):  
High Resolution ◽  
Three Dimensional ◽  
Linear Attenuation Coefficient ◽  
High Resolution Imaging ◽  
Mitochondrial Matrix ◽  
Morphological Parameter ◽  
Mitochondrial Membranes ◽  
X Ray ◽  
Resolution Imaging ◽  
Neuronal Disorders

AbstractMitochondria are dynamic organelles that change morphology to adapt to cellular energetic demands under both physiological and stress conditions. Cardiomyopathies and neuronal disorders are associated with structure-related dysfunction in mitochondria, but three-dimensional characterizations of the organelles are still lacking. In this study, we combined high-resolution imaging and 3D electron density information provided by cryo-soft X-ray tomography to characterize mitochondria cristae morphology isolated from murine. Using the linear attenuation coefficient, the mitochondria were identified (0.247 ± 0.04 µm−1) presenting average dimensions of 0.90 ± 0.20 µm in length and 0.63 ± 0.12 µm in width. The internal mitochondria structure was successfully identified by reaching up the limit of spatial resolution of 35 nm. The internal mitochondrial membranes invagination (cristae) complexity was calculated by the mitochondrial complexity index (MCI) providing quantitative and morphological information of mitochondria larger than 0.90 mm in length. The segmentation to visualize the cristae invaginations into the mitochondrial matrix was possible in mitochondria with MCI ≥ 7. Altogether, we demonstrated that the MCI is a valuable quantitative morphological parameter to evaluate cristae modelling and can be applied to compare healthy and disease state associated to mitochondria morphology.

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