Three dimensional arrangement of mitochondria and endoplasmic reticulum in the heart muscle fiber of the rat

1981 ◽  
Vol 200 (2) ◽  
pp. 139-151 ◽  
Author(s):  
D. Segretain ◽  
A. Rambourg ◽  
Y. Clermont
Keyword(s):  
Endoplasmic Reticulum ◽  
Muscle Fiber ◽  
Heart Muscle ◽  
Three Dimensional

scholarly journals Structure of the Lectin Mannose 6-Phosphate Receptor Homology (MRH) Domain of Glucosidase II, an Enzyme That Regulates Glycoprotein Folding Quality Control in the Endoplasmic Reticulum

2013 ◽  
Vol 288 (23) ◽  
pp. 16460-16475 ◽  
Author(s):  
Linda J. Olson ◽  
Ramiro Orsi ◽  
Solana G. Alculumbre ◽  
Francis C. Peterson ◽  
Ivan D. Stigliano ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Three Dimensional ◽  
Binding Pocket ◽  
Dimensional Structure ◽  
Mannose Residue ◽  
Glucosidase Ii ◽  
Mannose 6 Phosphate ◽  
First Time ◽  
Conserved Residue

Here we report for the first time the three-dimensional structure of a mannose 6-phosphate receptor homology (MRH) domain present in a protein with enzymatic activity, glucosidase II (GII). GII is involved in glycoprotein folding in the endoplasmic reticulum. GII removes the two innermost glucose residues from the Glc3Man9GlcNAc2 transferred to nascent proteins and the glucose added by UDP-Glc:glycoprotein glucosyltransferase. GII is composed of a catalytic GIIα subunit and a regulatory GIIβ subunit. GIIβ participates in the endoplasmic reticulum localization of GIIα and mediates in vivo enhancement of N-glycan trimming by GII through its C-terminal MRH domain. We determined the structure of a functional GIIβ MRH domain by NMR spectroscopy. It adopts a β-barrel fold similar to that of other MRH domains, but its binding pocket is the most shallow known to date as it accommodates a single mannose residue. In addition, we identified a conserved residue outside the binding pocket (Trp-409) present in GIIβ but not in other MRHs that influences GII glucose trimming activity.

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...

Three-dimensional organization of endoplasmic reticulum in the ventral photoreceptors ofLimulus

1994 ◽  
Vol 341 (2) ◽  
pp. 172-183 ◽  
Author(s):  
Jane J. Feng ◽  
John H. Carson ◽  
Frank Morgan ◽  
Bernd Walz ◽  
Alan Fein
Keyword(s):  
Endoplasmic Reticulum ◽  
Three Dimensional

Electrical turbulence in three-dimensional heart muscle

Science ◽  
1994 ◽  
Vol 266 (5187) ◽  
pp. 1003-1006 ◽  
Author(s):  
A. Winfree
Keyword(s):  
Heart Muscle ◽  
Three Dimensional

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 Combined diffusion and strain tensor MRI reveals a heterogeneous, planar pattern of strain development during isometric muscle contraction

2011 ◽  
Vol 300 (5) ◽  
pp. R1079-R1090 ◽  
Author(s):  
Erin K. Englund ◽  
Christopher P. Elder ◽  
Qing Xu ◽  
Zhaohua Ding ◽  
Bruce M. Damon
Keyword(s):  
Muscle Contraction ◽  
Muscle Fiber ◽  
Diffusion Tensor ◽  
Strain Tensor ◽  
Three Dimensional ◽  
Fiber Direction ◽  
Strain Pattern ◽  
Isometric Muscle Contraction ◽  
Diffusion Tensors

The purposes of this study were to create a three-dimensional representation of strain during isometric contraction in vivo and to interpret it with respect to the muscle fiber direction. Diffusion tensor MRI was used to measure the muscle fiber direction of the tibialis anterior (TA) muscle of seven healthy volunteers. Spatial-tagging MRI was used to measure linear strains in six directions during separate 50% maximal isometric contractions of the TA. The strain tensor (E) was computed in the TA's deep and superficial compartments and compared with the respective diffusion tensors. Diagonalization of E revealed a planar strain pattern, with one nonzero negative strain (εN) and one nonzero positive strain (εP); both strains were larger in magnitude ( P < 0.05) in the deep compartment [εN = −40.4 ± 4.3%, εP = 35.1 ± 3.5% (means ± SE)] than in the superficial compartment (εN = −24.3 ± 3.9%, εP = 6.3 ± 4.9%). The principal shortening direction deviated from the fiber direction by 24.0 ± 1.3° and 39.8 ± 6.1° in the deep and superficial compartments, respectively ( P < 0.05, deep vs. superficial). The deviation of the shortening direction from the fiber direction was due primarily to the lower angle of elevation of the shortening direction over the axial plane than that of the fiber direction. It is concluded that three-dimensional analyses of strain interpreted with respect to the fiber architecture are necessary to characterize skeletal muscle contraction in vivo. The deviation of the principal shortening direction from the fiber direction may relate to intramuscle variations in fiber length and pennation angle.

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