scholarly journals Coronaviruses construct an interconnection way with ERAD and autophagy

2021 ◽  
Author(s):  
Aref Movaqar ◽  
Atieh Yaghoubi ◽  
SA Rahim Rezaee ◽  
Saeid A Jamehdar ◽  
Saman Soleimanpour
Keyword(s):  
Communication Network ◽  
Endoplasmic Reticulum ◽  
Infected Cell ◽  
Protein Degradation ◽  
Structural Features ◽  
Degradation Pathways ◽  
Comprehensive Review ◽  
Large Numbers ◽  
Intracellular Mechanism ◽  
Virus Distribution

Coronaviruses quickly became a pandemic or epidemic, affecting large numbers of humans, due to their structural features and also because of their impacts on intracellular communications. The knowledge of the intracellular mechanism of virus distribution could help understand the coronavirus’s proper effects on different pathways that lead to the infections. They protect themselves from recognition and damage the infected cell by using an enclosed membrane through hijacking the autophagy and endoplasmic reticulum-associated protein degradation pathways. The present study is a comprehensive review of the coronavirus strategy in upregulating the communication network of autophagy and endoplasmic reticulum-associated protein degradation.

scholarly journals The Png1–Rad23 complex regulates glycoprotein turnover

2006 ◽  
Vol 172 (2) ◽  
pp. 211-219 ◽  
Author(s):  
Ikjin Kim ◽  
Jungmi Ahn ◽  
Chang Liu ◽  
Kaori Tanabe ◽  
Jennifer Apodaca ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Substrate Specificity ◽  
Protein Degradation ◽  
Binding Proteins ◽  
Degradation Pathways ◽  
Ricin A Chain ◽  
Substrate Degradation ◽  
A Chain ◽  
Specific Degradation ◽  
Ricin A

Misfolded proteins in the endoplasmic reticulum (ER) are destroyed by a pathway termed ER-associated protein degradation (ERAD). Glycans are often removed from glycosylated ERAD substrates in the cytosol before substrate degradation, which maintains the efficiency of the proteasome. Png1, a deglycosylating enzyme, has long been suspected, but not proven, to be crucial in this process. We demonstrate that the efficient degradation of glycosylated ricin A chain requires the Png1–Rad23 complex, suggesting that this complex couples protein deglycosylation and degradation. Rad23 is a ubiquitin (Ub) binding protein involved in the transfer of ubiquitylated substrates to the proteasome. How Rad23 achieves its substrate specificity is unknown. We show that Rad23 binds various regulators of proteolysis to facilitate the degradation of distinct substrates. We propose that the substrate specificity of Rad23 and other Ub binding proteins is determined by their interactions with various cofactors involved in specific degradation pathways.

Analysis of the Anterior Secretory Cells of Onchidohs Muricata (Nudibranchia)

1981 ◽  
Vol 39 ◽  
pp. 614-615
Author(s):  
Roy Skidmore
Keyword(s):  
Endoplasmic Reticulum ◽  
Secretory Granules ◽  
Golgi Body ◽  
The Body ◽  
Secretory Cells ◽  
Secretory Vesicles ◽  
High Magnification ◽  
Large Numbers ◽  
Membrane Bound ◽  
Sole Of The Foot

The long-necked secretory cells in Onchidoris muricata are distributed in the anterior sole of the foot. These cells are interspersed among ciliated columnar and conical cells as well as short-necked secretory gland cells. The long-necked cells contribute a significant amount of mucoid materials to the slime on which the nudibranch travels. The body of these cells is found in the subepidermal tissues. A long process extends across the basal lamina and in between cells of the epidermis to the surface of the foot. The secretory granules travel along the process and their contents are expelled by exocytosis at the foot surface.The contents of the cell body include the nucleus, some endoplasmic reticulum, and an extensive Golgi body with large numbers of secretory vesicles (Fig. 1). The secretory vesicles are membrane bound and contain a fibrillar matrix. At high magnification the similarity of the contents in the Golgi saccules and the secretory vesicles becomes apparent (Fig. 2).

Localization of Intracisternal a Particle Antigens in Neoplastic Cells and Preimplantation Mouse Embryos

1980 ◽  
Vol 38 ◽  
pp. 696-697
Author(s):  
Thomas T.F. Huang ◽  
Patricia G. Calarco
Keyword(s):  
Endoplasmic Reticulum ◽  
Normal Development ◽  
Mouse Embryos ◽  
Neoplastic Cells ◽  
Large Numbers ◽  
Preimplantation Mouse Embryos ◽  
Preimplantation Mouse ◽  
Intracisternal A Particle ◽  
Normal Feature

The stage specific appearance of a retravirus, termed the Intracisternal A particle (IAP) is a normal feature of early preimplantation development. To date, all feral and laboratory strains of Mus musculus and even Asian species such as Mus cervicolor and Mus pahari express the particles during the 2-8 cell stages. IAP form by budding into the endoplasmic reticulum and appear singly or as groups of donut-shaped particles within the cisternae (fig. 1). IAP are also produced in large numbers in several neoplastic cells such as certain plasmacytomas and rhabdomyosarcomas. The role of IAP, either in normal development or in neoplastic behavior, is unknown.

scholarly journals Characterization of Endoplasmic Reticulum (ER) in Human Pluripotent Stem Cells Revealed Increased Susceptibility to Cell Death upon ER Stress

Cells ◽  
2020 ◽  
Vol 9 (5) ◽  
pp. 1078
Author(s):  
Tae Won Ha ◽  
Ji Hun Jeong ◽  
HyeonSeok Shin ◽  
Hyun Kyu Kim ◽  
Jeong Suk Im ◽  
...  
Keyword(s):  
Stem Cells ◽  
Endoplasmic Reticulum ◽  
Er Stress ◽  
Pluripotent Stem Cells ◽  
Meta Analysis ◽  
Embryonic Stem ◽  
Structural Features ◽  
Human Pluripotent Stem Cells ◽  
Differentiated Cells ◽  
Induced Apoptosis

Human pluripotent stem cells (hPSCs), such as embryonic stem cells (ESCs) and induced pluripotent stem cells (iPSCs), have a well-orchestrated program for differentiation and self-renewal. However, the structural features of unique proteostatic-maintaining mechanisms in hPSCs and their features, distinct from those of differentiated cells, in response to cellular stress remain unclear. We evaluated and compared the morphological features and stress response of hPSCs and fibroblasts. Compared to fibroblasts, electron microscopy showed simpler/fewer structures with fewer networks in the endoplasmic reticulum (ER) of hPSCs, as well as lower expression of ER-related genes according to meta-analysis. As hPSCs contain low levels of binding immunoglobulin protein (BiP), an ER chaperone, thapsigargin treatment sharply increased the gene expression of the unfolded protein response. Thus, hPSCs with decreased chaperone function reacted sensitively to ER stress and entered apoptosis faster than fibroblasts. Such ER stress-induced apoptotic processes were abolished by tauroursodeoxycholic acid, an ER-stress reliever. Hence, our results revealed that as PSCs have an underdeveloped structure and express fewer BiP chaperone proteins than somatic cells, they are more susceptible to ER stress-induced apoptosis in response to stress.

scholarly journals Endoplasmic Reticulum-Localized Amyloid beta-Peptide is Degraded in the Cytosol by Two Distinct Degradation Pathways

Traffic ◽  
2004 ◽  
Vol 5 (2) ◽  
pp. 89-101 ◽  
Author(s):  
Anton Schmitz ◽  
Andrea Schneider ◽  
Markus P. Kummer ◽  
Volker Herzog
Keyword(s):  
Endoplasmic Reticulum ◽  
Amyloid Beta ◽  
Amyloid Beta Peptide ◽  
Degradation Pathways ◽  
Beta Peptide

Structure of the chloroplast and its DNA in chloromonadophycean algae

1981 ◽  
Vol 49 (1) ◽  
pp. 401-409
Author(s):  
A.W. Coleman ◽  
P. Heywood
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Membrane ◽  
Nuclear Envelope ◽  
Chloroplast Dna ◽  
Single Layer ◽  
Longitudinal Axis ◽  
Chloroplast Envelope ◽  
Large Numbers ◽  
Gonyostomum Semen ◽  
Chloroplast Stroma

The arrangement and ultrastructure of chloroplasts is described for the Chloromonadophycean algae gonyostomum semen Diesing and Vacuolaria virescens Cienkowsky. The chloroplasts are present in large numbers and are discoid structures approximately 3–4 micrometer in length by 2–3 micrometer in width. In Gonyostomum semen the chloroplasts form a single layer immediately interior to the cell membrane; frequently their longitudinal axis parallels the longitudinal axis of the cell. The chloroplasts in Vacuolaria virescens are more than I layer deep and do not appear to be preferentially oriented. In both organisms, chloroplast bands usually consist of 3 apposed thylakoids, although fusion and interconnections between adjacent bands frequently occur. External to the girdle band (the outermost thylakoids) is the chloroplast envelope. This is bounded by endoplasmic reticulum but there is no immediately apparent continuity between this endoplasmic reticulum and the nuclear envelope. Electron-dense spheres in the chloroplast stroma are thought to be lipid food reserve. Ring-shaped electron-translucent regions in the chloroplast contain chloroplast DNA. The DNA is distributed along this ring in an uneven fashion and, when stained, resembles a string of beads. Each plastid has I ring, and the ring is unbroken in the intact plastid.

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