Structural features of influenza virus neuraminidase (NA) required for translocation across the rough endoplasmic reticulum (RER) and transport to the plasma membrane

1985 ◽  
Vol 3 ◽  
pp. 7
Author(s):  
N. Sivasubramanian ◽  
T.J. Bos ◽  
D.P. Nayak
Development ◽  
1978 ◽  
Vol 43 (1) ◽  
pp. 247-261
Author(s):  
Par Anne-Marie Bautz

The morphogenesis of the abdominal epidermis in Calliphora erythrocephala begins by a cellular proliferation which proceeds slowly in larvae and rapidly in pupae. This allows histoblasts to glide and invade the whole abdominal surface. As soon as the new epidermal sheet has become continuous, differentiation begins. Generalized epidermal cells show an intense activity which leads to the deposition of imaginal cuticle from the 6th day after pupation onwards. After cuticle deposition they darken and become inactive although they remain alive, even after emergence. Trichogen and tormogen cells are even more active than generalized epidermal cells, especially the trichogen cell in which polyribosomes and microtubules are abundant. The former are possibly involved in microtubule synthesis. After cuticle deposition the trichogen and tormogen cells undergo degeneration. Their nuclei contract, rough endoplasmic reticulum breaks down and cytoplasm breaks up into fragments through infoldings which proliferate from the plasma membrane. Finally only generalized epidermal cells and sensory cells remain alive in the adult.


1976 ◽  
Vol 24 (6) ◽  
pp. 713-724 ◽  
Author(s):  
F Roels

In sheep hepatocytes catalase activity was demonstrated both within peroxisomes and within the cytosol. In the cytosol the catalase reaction product is contiguous to the plasma membrane and surrounds the nuclei, rough endoplasmic reticulum, cisternae, mitochondria and Golgi apparatus. This is the first cytochemical demonstration of guine extraperoxisomal catalase. No catalase reaction product was seen in the cytosol of nonparenchymal cells. To demonstrate catalase, both glutaraldehyde and formaldehyde fixation were used, followed by a diaminobenzidine technique modified from Novikoff and Goldfischer. Control reactions were performed to distinguish catalase reaction product from adsorption of oxidized diaminobenzidine and from precipitate due to oxidase-, peroxidase- or heat-stable peroxidatic activities. The results were evaluated in the light and electron microscopes.


1990 ◽  
Vol 68 (7) ◽  
pp. 1454-1467 ◽  
Author(s):  
K. M. Fry ◽  
S. B. McIver

Light and electron microscopy were used to observe development of the lateral palatal brush in Aedes aegypti (L.) larvae. Development was sampled at 4-h intervals from second- to third-instar ecdyses. Immediately after second-instar ecdysis, the epidermis apolyses from newly deposited cuticle in the lateral palatal pennicular area to form an extensive extracellular cavity into which the fourth-instar lateral palatal brush filaments grow as cytoplasmic extensions. On reaching their final length, the filaments deposit cuticulin, inner epicuticle, and procuticle sequentially on their outer surfaces. The lateral palatal crossbars, on which the lateral palatal brush filaments insert, form after filament development is complete. At the beginning of development, the organelles involved in plasma membrane and cuticle production are located at the base and middle of the cells. As the filament rudiments grow, most rough endoplasmic reticulum, mitochondria, and Golgi apparatus move to the apex of the epidermal cells and into the filament rudiments. After formation of the lateral palatal brush filaments and lateral palatal crossbars, extensive organelle breakdown occurs. Lateral palatal brush formation is unusual in that no digestion and resorption of old endocuticle occurs prior to deposition of new cuticle. No mucopolysaccharide secretion by the lateral palatal brush epidermis was observed, nor were muscle fibres observed to attach to the lateral palatal crossbars, as has been suggested by other workers.


2017 ◽  
Vol 8 (1) ◽  
Author(s):  
Isabel Fernández de Castro Martin ◽  
Guillaume Fournier ◽  
Martin Sachse ◽  
Javier Pizarro-Cerda ◽  
Cristina Risco ◽  
...  

1972 ◽  
Vol 11 (2) ◽  
pp. 477-489
Author(s):  
A. S. BREATHNACH ◽  
C. STOLINSKI ◽  
M. GROSS

Fresh, chemically unfixed, glycerinated specimens of mouse liver were examined by the technique of freeze-fracture replication without sublimation (i.e. they were not ‘etched’). Where extensive areas of fractured lamellar membranes of the rough endoplasmic reticulum are revealed en face, 2 types of fracture face are distinguishable. One of these fracture faces (A) is directed towards the cytoplasm, and the other (B) towards the cisternal cavity. A characteristic mosaic, or patchwork pattern of flat areas circumscribed by particles, is evident on both faces, and more clearly so on face B, due to a greater number of more prominent particles. Similar mosaic patterns are revealed on convex faces of the nuclear membrane, and on concave fracture faces of mitochondrial membranes, but are not evident on fracture faces of the plasma membrane. Uncertainty in establishing the exact plane of fracture of membranes in this material, since glycerol is virtually non-sublimable, makes it difficult to assess the significance of these mosaic patterns. The fact that ribosomes are not identifiable on either face of fractured endoplasmic reticulum membranes, gives no certain indication of the plane of fracture.


1984 ◽  
Vol 99 (3) ◽  
pp. 1101-1109 ◽  
Author(s):  
A A Rogalski ◽  
J E Bergmann ◽  
S J Singer

We studied the effects of changes in microtubule assembly status upon the intracellular transport of an integral membrane protein from the rough endoplasmic reticulum to the plasma membrane. The protein was the G glycoprotein of vesicular stomatitis virus in cells infected with the Orsay-45 temperature-sensitive mutant of the virus; the synchronous intracellular transport of the G protein could be initiated by a temperature shift-down protocol. The intracellular and surface-expressed G protein were separately detected and localized in the same cells at different times after the temperature shift, by double-immunofluorescence microscopic measurements, and the extent of sialylation of the G protein at different times was quantitated by immunoprecipitation and SDS PAGE of [35S]methionine-labeled cell extracts. Neither complete disassembly of the cytoplasmic microtubules by nocodazole treatment, nor the radical reorganization of microtubules upon taxol treatment, led to any perceptible changes in the rate or extent of G protein sialylation, nor to any marked changes in the rate or extent of surface appearance of the G protein. However, whereas in control cells the surface expression of G was polarized, at membrane regions in juxtaposition to the perinuclear compact Golgi apparatus, in cells with disassembled microtubules the surface expression of the G protein was uniform, corresponding to the intracellular dispersal of the elements of the Golgi apparatus. The mechanisms of transfer of integral proteins from the rough endoplasmic reticulum to the Golgi apparatus, and from the Golgi apparatus to the plasma membrane, are discussed in the light of these observations, and compared with earlier studies of the intracellular transport of secretory proteins.


1996 ◽  
Vol 16 (5) ◽  
pp. 1946-1954 ◽  
Author(s):  
L V Lotti ◽  
L Lanfrancone ◽  
E Migliaccio ◽  
C Zompetta ◽  
G Pelicci ◽  
...  

The intracellular localization of Shc proteins was analyzed by immunofluorescence and immunoelectron microscopy in normal cells and cells expressing the epidermal growth factor receptor or the EGFR/erbB2 chimera. In unstimulated cells, the immunolabeling was localized in the central perinuclear area of the cell and mostly associated with the cytosolic side of rough endoplasmic reticulum membranes. Upon epidermal growth factor treatment and receptor tyrosine kinase activation, the immunolabeling became peripheral and was found to be associated with the cytosolic surface of the plasma membrane and endocytic structures, such as coated pits and endosomes, and with the peripheral cytosol. Receptor activation in cells expressing phosphorylation-defective mutants of Shc and erbB-2 kinase showed that receptor autophosphorylation, but not Shc phosphorylation, is required for redistribution of Shc proteins. The rough endoplasmic reticulum localization of Shc proteins in unstimulated cells and their massive recruitment to the plasma membrane, endocytic structures, and peripheral cytosol following receptor tyrosine kinase activation could account for multiple putative functions of the adaptor protein.


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