Role of Intracellular Distribution of Feline and Bovine SAMHD1 Proteins in Lentiviral Restriction

2021 ◽  
Author(s):  
Chu Wang ◽  
Lina Meng ◽  
Jialin Wang ◽  
Kaikai Zhang ◽  
Sizhu Duan ◽  
...  
Keyword(s):  
Intracellular Distribution

The role of ferritin in the intracellular distribution of gallium 67

1984 ◽  
Vol 9 (5) ◽  
pp. 237-240 ◽  
Author(s):  
Kayoko Nakamura ◽  
Hajime Kawaguchi ◽  
Kimi Shimizu ◽  
Hirotake Orii
Keyword(s):  
Intracellular Distribution ◽  
Gallium 67

Meiotic maturation of mouse oocytes in vitro: association of newly synthesized proteins with condensing chromosomes

1976 ◽  
Vol 20 (3) ◽  
pp. 549-568 ◽  
Author(s):  
P.M. Wassarman ◽  
G.E. Letourneau
Keyword(s):  
Protein Synthesis ◽  
Mammalian Species ◽  
Germinal Vesicle ◽  
Chromosome Condensation ◽  
Intracellular Distribution ◽  
Meiotic Maturation ◽  
Meiotic Progression ◽  
Mouse Oocytes

The nature, intracellular distribution, and role of proteins synthesized during meiotic maturation of mouse oocytes in vitro have been examined. Proteins synthesized during the initial stages of maturation are concentrated within the nucleus (germinal vesicle) and become intimately associated with the condensing chromosomes. Inhibition of protein synthesis during this period does not prevent germinal vesicle dissolution or chromosome condensation, but meiotic progression is blocked reversibly at the circular bivalent stage. A protein is synthesized during meiotic maturation of the mouse oocyte which exhibits several of the characteristics of the very lysine-rich histone, FI; this and other histones are phosphorylated during the initial stages of maturation. These results are discussed in relation to studies of meiotic maturation of oocytes from non-mammalian species and chromosome condensation in both oocytes and mitotic cells.

Schmallenberg virus non-structural protein NSm: Intracellular distribution and role of non-hydrophobic domains

Virology ◽  
2018 ◽  
Vol 516 ◽  
pp. 46-54 ◽  
Author(s):  
Franziska Kraatz ◽  
Kerstin Wernike ◽  
Sven Reiche ◽  
Andrea Aebischer ◽  
Ilona Reimann ◽  
...  
Keyword(s):  
Intracellular Distribution ◽  
Schmallenberg Virus ◽  
Structural Protein

wingless signal and Zeste-white 3 kinase trigger opposing changes in the intracellular distribution of Armadillo

Development ◽  
1994 ◽  
Vol 120 (2) ◽  
pp. 369-380 ◽  
Author(s):  
M. Peifer ◽  
D. Sweeton ◽  
M. Casey ◽  
E. Wieschaus
Keyword(s):  
Signal Transduction ◽  
Genetic Analysis ◽  
Cell Fate ◽  
Intracellular Distribution ◽  
Beta Catenin ◽  
Signal Transduction System ◽  
Protein Levels ◽  
Wingless Signaling

wingless/wnt-1 signaling directs cell fate during development. Genetic analysis in Drosophila identified genes that may encode components of the wingless signal transduction system. Drosophila Armadillo, homolog of vertebrate beta-catenin, is required for wingless signaling. Unlike armadillo RNA, Armadillo protein accumulates non-uniformly in different cells of each embryonic segment. We found that cells alter their intracellular distribution of Armadillo in response to Wingless signal, accumulating increased levels of cytoplasmic Armadillo relative to those of membrane-associated protein. Levels of cytoplasmic Armadillo are also regulated by Zeste-White 3 kinase. Analysis of double mutants demonstrates that Armadillo's role in wingless signaling is direct, and that Armadillo functions downstream of both wingless and zeste-white 3. We present a model for the role of Armadillo stripes in transduction of wingless signal.

Critical role of evolutionarily conserved glycosylation at Asn211 in the intracellular trafficking and activity of sialyltransferase ST3Gal-II

2015 ◽  
Vol 469 (1) ◽  
pp. 83-95 ◽  
Author(s):  
Fernando M. Ruggiero ◽  
Aldo A. Vilcaes ◽  
Ramiro Iglesias-Bartolomé ◽  
José L. Daniotti
Keyword(s):  
Enzymatic Activity ◽  
Intracellular Trafficking ◽  
Critical Role ◽  
Intracellular Distribution ◽  
Evolutionarily Conserved

ST3Gal-II is largely responsible for ganglioside terminal α2,3-sialylation in mammals. We demonstrated that ST3Gal-II mainly distributes in proximal Golgi compartments and that the inhibition of N-glycosylation and oligosaccharide trimming is critical for its enzymatic activity and intracellular distribution.

scholarly journals Role of perilipins in the development of fatty liver disease.

2019 ◽  
Vol 2 (1) ◽  
Author(s):  
Erica Kubascik ◽  
Madison DeGoey ◽  
Dr. Gupta ◽  
Dr. Kostrominova
Keyword(s):  
Liver Disease ◽  
Fatty Liver ◽  
High Fat Diet ◽  
Fatty Liver Disease ◽  
Intracellular Distribution ◽  
Nonalcoholic Fatty Liver ◽  
Intracellular Receptor ◽  
The Impact ◽  
Oligomerization Domain

Background and Hypothesis: Lipid droplets (LDs) are fatty acid (FA) containing structures within cells. In obesity, hepatic LDs accumulate more FA which may cause steatosis and nonalcoholic fatty liver disease (NAFLD). Perilipins (PLINs) are a family of LDassociated proteins involved in intracellular trafficking and signaling. In hepatocytes, NAFLD alters expression of PLINs. Using metabolomics, Dr. Gupta’s laboratory previously showed enlarged LDs and altered PLIN1, 3, and 4 content in NOD2-/- compared to wild type (WT) mice on high fat diet (HFD). Nucleotide-binding and oligomerization domain (NOD) is an intracellular receptor that regulates sensitivity to obesity. To expand on Dr. Gupta’s study, we quantified diet-induced alterations and visualized intracellular distribution of PLINs in mouse livers. We hypothesized that PLIN2, 3, and 4 concentrations would increase whereas PLIN1 would decrease in NOD2-/-HFD compared to WTHFD mice. Methods: Immunostaining was used to visualize intracellular distribution of PLINs. Western blotting was used to quantify differences in PLINs protein expression.  Results: LD distribution showed WT regular chow (RC) = NOD2-/-RC < WTHFD<<NOD2-/-HFD. Bright LD-associated staining for PLIN2 was observed in both small and large LDs in all four groups. PLIN3 brightly stained the bile ducts, and it stained small LDs but not large LDs. PLIN4 stained small intracellular LDs in all four groups. PLIN1 showed a trend for decrease in both NOD2-/-HFD and WTHFD compared with RC mice. PLIN2 appears to be decreased in WTHFD and both NOD2-/- groups compared to WTRC. PLIN3 seemed to show increased expression in WTHFD but not in NOD2-/-. PLIN4 showed a trend for decreased expression in both NOD2-/-RC and NOD2-/-HFD mice compared to WTRC. Conclusion: Despite enlarged LD size, there was no detectable increase in PLINs expression in NOD2-/-HFD compared to WTHFD. This may be due to the impact of other LDassociated proteins in the livers of NOD2-/- mice.

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