Abstract 4144: The treatment with a derivative of Vitamin A (ATRA) modulates the expression and subcellular localization of Protein Kinase C (PKC) delta and induces growth inhibition in normal and tumor derived mammary cells

Author(s):  
Damian E. Berardi ◽  
María I. Díaz Bessone ◽  
Elisa D. Bal de Kier Joffé ◽  
Laura B. Todaro ◽  
Alejandro J. Urtreger
2019 ◽  
Vol 125 (Suppl_1) ◽  
Author(s):  
John P Morrow ◽  
Leroy C Joseph ◽  
Michael V Reyes ◽  
Konstaninos Drosatos

2019 ◽  
Vol 374 (1767) ◽  
pp. 20180315 ◽  
Author(s):  
Lina Lu ◽  
Qi Wang ◽  
Deqing Huang ◽  
Qiufang Xu ◽  
Xueping Zhou ◽  
...  

Rice black-streaked dwarf virus (RBSDV) was known to be transmitted by the small brown planthopper (SBPH) in a persistent, circulative and propagative manner in nature. Here, we show that RBSDV major outer capsid protein (also known as P10) suppresses the protein kinase C (PKC) activity of SBPH through interacting with the receptor for activated protein kinase C 1 (LsRACK1). The N terminal of P10 (amino acids (aa) 1–270) and C terminal of LsRACK1 (aa 268–315) were mapped as crucial for the interaction. Confocal microscopy and subcellular fractionation showed that RBSDV P10 fused to enhanced green fluorescent protein formed vesicular structures associated with endoplasmic reticulum (ER) membranes in Spodoptera frugiperda nine cells. Our results also indicated that RBSDV P10 retargeted the initial subcellular localization of LsRACK1 from cytoplasm and cell membrane to ER and affected the function of LsRACKs to activate PKC. Inhibition of RACK1 by double stranded RNA-induced gene silencing significantly promoted the replication of RBSDV in SBPH. In addition, the PKC pathway participates in the antivirus innate immune response of SBPH. This study highlights that RACK1 negatively regulates the accumulation of RBSDV in SBPH through activating the PKC signalling pathway, and RBSDV P10 changes the subcellular localization of LsRACK1 and affects its function to activate PKC. This article is part of the theme issue ‘Biotic signalling sheds light on smart pest management’.


1995 ◽  
Vol 96 (1) ◽  
pp. 31-35 ◽  
Author(s):  
Wei Zhang ◽  
Ronald E. Lawa ◽  
David R. Hintona ◽  
Yuzhuang Su ◽  
William T. Couldwell

1999 ◽  
Vol 274 (10) ◽  
pp. 6461-6468 ◽  
Author(s):  
Amelia S. Edwards ◽  
Maree C. Faux ◽  
John D. Scott ◽  
Alexandra C. Newton

1994 ◽  
Vol 5 (8) ◽  
pp. 907-920 ◽  
Author(s):  
N T Goode ◽  
M A Hajibagheri ◽  
G Warren ◽  
P J Parker

Mammalian protein kinase C (PKC) isotypes elicit a number of effects on expression in Schizosaccharomyces pombe. A small decrease in growth rate results from PKC-gamma expression, and treatment of these cells with phorbol esters leads to marked growth inhibition and vesicle formation. PKC-delta and -eta expression causes growth inhibition and vesiculation, and the magnitude of both of these effects is increased by phorbol esters. In contrast, PKC-epsilon expression produces growth inhibition but no vesicle accumulation, and this effect is not responsive to phorbol ester. Finally, PKC-zeta has no observable effect. Thus, isotype-specific biological effects are observed. The accumulation of vesicles correlates with phorbol ester-dependent growth inhibition and occurs only with expression of those isotypes that down-regulate in response to phorbol esters in these cells. Antibodies against mammalian clathrin light chain 1a identified clathrin-coated vesicles and up-regulation of clathrin expression in those cells where vesicles accumulate; the increased vesicular traffic includes an element of endocytosis. Thus expression of specific mammalian PKC isotypes up-regulates endocytosis in S. pombe, providing a likely explanation for PKC-mediated receptor internalization in higher eukaryotes.


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