MicroRNA-275 directly targets sarco/endoplasmic reticulum Ca2+adenosine triphosphatase (SERCA) to control key functions in the mosquito gut

2016 ◽  
Author(s):  
Bo Zhao
Keyword(s):  
Endoplasmic Reticulum ◽  
Adenosine Triphosphatase

scholarly journals The medial-Golgi Ion Pump Pmr1 Supplies the Yeast Secretory Pathway with Ca2+ and Mn2+ Required for Glycosylation, Sorting, and Endoplasmic Reticulum-Associated Protein Degradation

1998 ◽  
Vol 9 (5) ◽  
pp. 1149-1162 ◽  
Author(s):  
Gabriele Dürr ◽  
Jochen Strayle ◽  
Richard Plemper ◽  
Saskia Elbs ◽  
Saskia K. Klee ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Adenosine Triphosphatase ◽  
Intracellular Transport ◽  
Secretory Pathway ◽  
Protein Glycosylation ◽  
Carboxypeptidase Y ◽  
Dual Function ◽  
Ion Pump ◽  
Endoplasmic Reticulum Protein ◽  
Sorting Receptor

The yeast Ca2+ adenosine triphosphatase Pmr1, located in medial-Golgi, has been implicated in intracellular transport of Ca2+ and Mn2+ ions. We show here that addition of Mn2+ greatly alleviates defects ofpmr1 mutants in N-linked and O-linked protein glycosylation. In contrast, accurate sorting of carboxypeptidase Y (CpY) to the vacuole requires a sufficient supply of intralumenal Ca2+. Most remarkably, pmr1 mutants are also unable to degrade CpY*, a misfolded soluble endoplasmic reticulum protein, and display phenotypes similar to mutants defective in the stress response to malfolded endoplasmic reticulum proteins. Growth inhibition of pmr1 mutants on Ca2+-deficient media is overcome by expression of other Ca2+ pumps, including a SERCA-type Ca2+ adenosine triphosphatase from rabbit, or by Vps10, a sorting receptor guiding non-native luminal proteins to the vacuole. Our analysis corroborates the dual function of Pmr1 in Ca2+ and Mn2+ transport and establishes a novel role of this secretory pathway pump in endoplasmic reticulum-associated processes.

scholarly journals MicroRNA-275 targets sarco/endoplasmic reticulum Ca2+ adenosine triphosphatase (SERCA) to control key functions in the mosquito gut

PLoS Genetics ◽  
2017 ◽  
Vol 13 (8) ◽  
pp. e1006943 ◽  
Author(s):  
Bo Zhao ◽  
Keira J. Lucas ◽  
Tusar T. Saha ◽  
Jisu Ha ◽  
Lin Ling ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Adenosine Triphosphatase

scholarly journals Tail-anchored PEX26 targets peroxisomes via a PEX19-dependent and TRC40-independent class I pathway

2013 ◽  
Vol 200 (5) ◽  
pp. 651-666 ◽  
Author(s):  
Yuichi Yagita ◽  
Takahide Hiromasa ◽  
Yukio Fujiki
Keyword(s):  
Amino Acids ◽  
Endoplasmic Reticulum ◽  
Membrane Protein ◽  
Adenosine Triphosphatase ◽  
Transmembrane Domain ◽  
Peroxisomal Membrane ◽  
Basic Amino Acids ◽  
C Terminus ◽  
Peroxisomal Targeting ◽  
Ta Proteins

Tail-anchored (TA) proteins are anchored into cellular membranes by a single transmembrane domain (TMD) close to the C terminus. Although the targeting of TA proteins to peroxisomes is dependent on PEX19, the mechanistic details of PEX19-dependent targeting and the signal that directs TA proteins to peroxisomes have remained elusive, particularly in mammals. The present study shows that PEX19 formed a complex with the peroxisomal TA protein PEX26 in the cytosol and translocated it directly to peroxisomes by interacting with the peroxisomal membrane protein PEX3. Unlike in yeast, the adenosine triphosphatase TRC40, which delivers TA proteins to the endoplasmic reticulum, was dispensable for the peroxisomal targeting of PEX26. Moreover, the basic amino acids within the luminal domain of PEX26 were essential for binding to PEX19 and thereby for peroxisomal targeting. Finally, our results suggest that a TMD that escapes capture by TRC40 and is followed by a highly basic luminal domain directs TA proteins to peroxisomes via the PEX19-dependent route.

scholarly journals Tissue-culture cell fractionation. Fractionation of cellular membranes from 125I/lactoperoxidase-labelled Lettrée cells homogenized by bicarbonate-induced lysis: resolution of membranes by zonal centrifugation and in sucrose and metrizamide gradients

1979 ◽  
Vol 182 (1) ◽  
pp. 173-180 ◽  
Author(s):  
J M Graham ◽  
K H M Coffey
Keyword(s):  
Endoplasmic Reticulum ◽  
Plasma Membrane ◽  
Adenosine Triphosphatase ◽  
Gradient Centrifugation ◽  
Culture Cell ◽  
Tissue Culture Cell ◽  
Cell Fractionation ◽  
Rate Gradient ◽  
Nadph Cytochrome C Reductase ◽  
Zonal Rotor

1. Lettrée cells were grown intraperitoneally in MF-1 mice and labelled extrinsically by the 125I/lactoperoxidase technique. 2. The cells were swollen in 1 mM-NaHCO3 and disrupted in a Dounce homogenizer. 3. Crude fractions of endoplasmic reticulum, plasma membrane and mitochondria were separated from a post-nuclear supernatant by sedimentation-rate gradient centrifugation in a BXIV zonal rotor. 4. Further resolution of these membranes was carried out in isopycnic sucrose gradients. 5. Bands of material from the latter were subfractionated in gradients of metrizamide. Some very pure subfractions of plasma membrane and endoplasmic reticulum were obtained. In addition, one subfraction containing 125I and NADPH-cytochrome c reductase but no Na++K+-stimulated adenosine triphosphatase and another containing these two enzymes but no 125I were resolved.

In Vitro Induction of Crystals of MT Protein by Vinblastine-Colcemid in Mouse Spermatids

1974 ◽  
Vol 32 ◽  
pp. 132-133
Author(s):  
John J. Wolosewick ◽  
John H. D. Bryan
Keyword(s):  
Endoplasmic Reticulum ◽  
Smooth Endoplasmic Reticulum ◽  
Nuclear Ring ◽  
Rough Er ◽  
Distal Direction ◽  
In Vitro Induction

Early in spermiogenesis the manchette is rapidly assembled in a distal direction from the nuclear-ring-densities. The association of vesicles of smooth endoplasmic reticulum (SER) and the manchette microtubules (MTS) has been reported. In the mouse, osmophilic densities at the distal ends of the manchette are the organizing centers (MTOCS), and are associated with the SER. Rapid MT assembly and the lack of rough ER suggests that there is an existing pool of MT protein. Colcemid potentiates the reaction of vinblastine with tubulin and was used in this investigation to detect this protein.

Ultrastructure of the Parotid Gland of the Nine-Banded Armadillo

1977 ◽  
Vol 35 ◽  
pp. 640-641
Author(s):  
J. R. Ruby
Keyword(s):  
Endoplasmic Reticulum ◽  
Parotid Gland ◽  
Periodic Acid ◽  
Acinar Cells ◽  
Duct System ◽  
Parotid Glands ◽  
Dasypus Novemcinctus ◽  
Anterior Portion ◽  
Periodic Acid Schiff ◽  
Thin Sections

Parotid glands were obtained from five adult (four male and one female) armadillos (Dasypus novemcinctus) which were perfusion-fixed. The glands were located in a position similar to that of most mammals. They extended interiorly to the anterior portion of the submandibular gland.In the light microscope, it was noted that the acini were relatively small and stained strongly positive with the periodic acid-Schiff (PAS) and alcian blue techniques, confirming the earlier results of Shackleford (1). Based on these qualities and other structural criteria, these cells have been classified as seromucous (2). The duct system was well developed. There were numerous intercalated ducts and intralobular striated ducts. The striated duct cells contained large amounts of PAS-positive substance.Thin sections revealed that the acinar cells were pyramidal in shape and contained a basally placed, slightly flattened nucleus (Fig. 1). The rough endoplasmic reticulum was also at the base of the cell.

Organisation in the Structure of the Cytoplasmic Ground Substance

1978 ◽  
Vol 36 (3) ◽  
pp. 627-639
Author(s):  
K.R. Porter
Keyword(s):  
Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Random Distribution ◽  
Ground Substance ◽  
The Matrix ◽  
Cell Processes ◽  
Cytoplasmic Ground Substance

Most types of cells are known from their structure and overall form to possess a characteristic organization. In some instances this is evident in the non-random disposition of organelles and such system subunits as cisternae of the endoplasmic reticulum or the Golgi complex. In others it appears in the distribution and orientation of cytoplasmic fibrils. And in yet others the organization finds expression in the non-random distribution and orientation of microtubules, especially as found in highly anisometric cells and cell processes. The impression is unavoidable that in none of these cases is the organization achieved without the involvement of the cytoplasmic ground substance (CGS) or matrix. This impression is based on the fact that a matrix is present and that in all instances these formed structures, whether membranelimited or filamentous, are suspended in it. In some well-known instances, as in arrays of microtubules which make up axonemes and axostyles, the matrix resolves itself into bridges (and spokes) between the microtubules, bridges which are in some cases very regularly disposed and uniform in size (Mcintosh, 1973; Bloodgood and Miller, 1974; Warner and Satir, 1974).

Ultrastructural Changes Associated with Alcoholic Hyalin in Hepatocytes and Biliary Epithelial Cells

1971 ◽  
Vol 29 ◽  
pp. 572-573
Author(s):  
Odell T. Minick ◽  
Hidejiro Yokoo ◽  
Fawzia Batti
Keyword(s):  
Endoplasmic Reticulum ◽  
Epithelial Cells ◽  
Liver Biopsy ◽  
Alcoholic Hepatitis ◽  
Ultrastructural Changes ◽  
Main Mass ◽  
Biliary Epithelial Cells ◽  
Biopsy Specimens ◽  
Alcoholic Hyalin

To learn more of the nature and origin of alcoholic hyalin (AH), 15 liver biopsy specimens from patients with alcoholic hepatitis were studied in detail.AH was found not only in hepatocytes but also in ductular cells (Figs. 1 and 2), although in the latter location only rarely. The bulk of AH consisted of a randomly oriented network of closely packed filaments measuring about 150 Å in width. Bundles of filaments smaller in diameter (40-90 Å) were observed along the periphery of the main mass (Fig. 1), often surrounding it in a rim-like fashion. Fine filaments were also found close to the nucleus in both hepatocytes and biliary epithelial cells, the latter even though characteristic AH was not present (Figs. 3 and 4). Dispersed among the larger filaments were glycogen, RNA particles and profiles of endoplasmic reticulum. Dilated cisternae of endoplasmic reticulum were often conspicuous around the periphery of the AH mass. A limiting membrane was not observed.

Compound Symbiosis in Peridinium Balticum

1973 ◽  
Vol 31 ◽  
pp. 500-501
Author(s):  
R. N. Tomas
Keyword(s):  
Endoplasmic Reticulum ◽  
Nuclear Envelope ◽  
The Other ◽  
Exact Nature ◽  
Symbiotic Relationship

Peridinium balticum appears to be unusual among the dinoflagellates in that it possesses two DNA-containing structures as determined by histochemical techniques. Ultrastructurally, the two dissimilar nuclei are contained within different protoplasts; one of the nuclei is characteristically dinophycean in nature, while the other is characteristically eucaryotic. The chloroplasts observed within P. balticum are intrinsic to an eucaryotic photosynthetic endosymbiont and not to the dinoflagellate. These organelles are surrounded by outpocketings of endoplasmic reticulum which are continuous with the eucaryotic nuclear envelope and are characterized by thylakoids composed of three apposed lamellae. Girdle lamellae and membranebounded interlamellar pyrenoids are also present. Only the plasmalemma of the endosymbiont segregates its protoplast from that of the dinophycean cytoplasm. The exact nature of this symbiotic relationship is at present not known.

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