Actin in Protein Synthesis and Protein Body Formation

2000 ◽  
pp. 129-143 ◽  
Author(s):  
Bratislav Stanković ◽  
Amy Clore ◽  
Shunnosuke Abe ◽  
Brian Larkins ◽  
Eric Davies
Keyword(s):  
Protein Synthesis ◽  
Protein Body ◽  
Body Formation

Ty1-fused protein-body formation for spatial organization of metabolic pathways inSaccharomyces cerevisiae

2017 ◽  
Vol 115 (3) ◽  
pp. 694-704 ◽  
Author(s):  
Jong Yun Han ◽  
Jae Myeong Song ◽  
Sung Hwa Seo ◽  
Chonglong Wang ◽  
Seung-Goo Lee ◽  
...  
Keyword(s):  
Metabolic Pathways ◽  
Spatial Organization ◽  
Protein Body ◽  
Body Formation

scholarly journals Nonredundant Function of Zeins and Their Correct Stoichiometric Ratio Drive Protein Body Formation in Maize Endosperm

2013 ◽  
Vol 162 (3) ◽  
pp. 1359-1369 ◽  
Author(s):  
X. Guo ◽  
L. Yuan ◽  
H. Chen ◽  
S. J. Sato ◽  
T. E. Clemente ◽  
...  
Keyword(s):  
Protein Body ◽  
Stoichiometric Ratio ◽  
Maize Endosperm ◽  
Body Formation

scholarly journals Opaque1 Encodes a Myosin XI Motor Protein That Is Required for Endoplasmic Reticulum Motility and Protein Body Formation in Maize Endosperm

2012 ◽  
Vol 24 (8) ◽  
pp. 3447-3462 ◽  
Author(s):  
Guifeng Wang ◽  
Fang Wang ◽  
Gang Wang ◽  
Fei Wang ◽  
Xiaowei Zhang ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Body ◽  
Motor Protein ◽  
Maize Endosperm ◽  
Body Formation ◽  
Myosin Xi

Effect of thefloury-2 locus on protein body formation during maize endosperm development

PROTOPLASMA ◽  
1992 ◽  
Vol 171 (3-4) ◽  
pp. 123-133 ◽  
Author(s):  
C. R. Lending ◽  
B. A. Larkins
Keyword(s):  
Protein Body ◽  
Endosperm Development ◽  
Maize Endosperm ◽  
Body Formation

Rice protein-body formation: all types are initiated by dilation of the endoplasmic reticulum

Planta ◽  
1982 ◽  
Vol 154 (2) ◽  
pp. 184-188 ◽  
Author(s):  
K. J. Oparka ◽  
N. Harris
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Body ◽  
Body Formation ◽  
Rice Protein

scholarly journals The Maize Floury1 Gene Encodes a Novel Endoplasmic Reticulum Protein Involved in Zein Protein Body Formation

2007 ◽  
Vol 19 (8) ◽  
pp. 2569-2582 ◽  
Author(s):  
David R. Holding ◽  
Marisa S. Otegui ◽  
Bailin Li ◽  
Robert B. Meeley ◽  
Thao Dam ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Body ◽  
Body Formation ◽  
Endoplasmic Reticulum Protein ◽  
Zein Protein

Higher accumulation of F1-V fusion recombinant protein in plants after induction of protein body formation

2009 ◽  
Vol 72 (1-2) ◽  
pp. 75-89 ◽  
Author(s):  
M. Lucrecia Alvarez ◽  
Emel Topal ◽  
Federico Martin ◽  
Guy A. Cardineau
Keyword(s):  
Recombinant Protein ◽  
Protein Body ◽  
Body Formation

scholarly journals Processing Body Formation Limits Proinflammatory Cytokine Synthesis in Endotoxin-Tolerant Monocytes and Murine Septic Macrophages

2015 ◽  
Vol 7 (6) ◽  
pp. 572-583 ◽  
Author(s):  
Clara McClure ◽  
Laura Brudecki ◽  
Zhi Q. Yao ◽  
Charles E. McCall ◽  
Mohamed El Gazzar
Keyword(s):  
Protein Synthesis ◽  
Rna Binding ◽  
Mrna Translation ◽  
Endotoxin Tolerance ◽  
Translational Repression ◽  
Binding Motif ◽  
Body Formation ◽  
Translational Repressor ◽  
Protein Levels ◽  
Repressor Complex

An anti-inflammatory phenotype with pronounced immunosuppression develops during sepsis, during which time neutrophils and monocytes/macrophages limit their Toll-like receptor 4 responses to bacterial lipopolysaccharide (LPS/endotoxin). We previously reported that during this endotoxin-tolerant state, distinct signaling pathways differentially repress transcription and translation of proinflammatory cytokines such as TNFα and IL-6. Sustained endotoxin tolerance contributes to sepsis mortality. While transcription repression requires chromatin modifications, a translational repressor complex of Argonaute 2 (Ago2) and RNA-binding motif protein 4 (RBM4), which bind the 3′-UTR of TNFα and IL-6 mRNA, limits protein synthesis. Here, we show that Dcp1 supports the assembly of the Ago2 and RBM4 repressor complex into cytoplasmic processing bodies (p-bodies) in endotoxin-tolerant THP-1 human monocytes following stimulation with LPS, resulting in translational repression and limiting protein synthesis. Importantly, this translocation process is reversed by Dcp1 knockdown, which restores TNFα and IL-6 protein levels. We also find this translational repression mechanism in primary macrophages of septic mice. Because p-body formation is a critical step in mRNA translation repression, we conclude that Dcp1 is a major component of the translational repression machinery of endotoxin tolerance and may contribute to sepsis outcome.

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