scholarly journals The specialized unfolded protein response of B lymphocytes: ATF6α-independent development of antibody-secreting B cells

2012 ◽  
Vol 51 (3-4) ◽  
pp. 347-355 ◽  
Author(s):  
Ileana V. Aragon ◽  
Robert A. Barrington ◽  
Suzanne Jackowski ◽  
Kazutoshi Mori ◽  
Joseph W. Brewer
Keyword(s):  
B Cells ◽  
Unfolded Protein Response ◽  
B Lymphocytes ◽  
Unfolded Protein ◽  
Protein Response

scholarly journals Rapid B Cell Receptor-induced Unfolded Protein Response in Nonsecretory B Cells Correlates with Pro-VersusAntiapoptotic Cell Fate

2005 ◽  
Vol 280 (48) ◽  
pp. 39762-39771 ◽  
Author(s):  
Alison H. Skalet ◽  
Jennifer A. Isler ◽  
Leslie B. King ◽  
Heather P. Harding ◽  
David Ron ◽  
...  
Keyword(s):  
B Cells ◽  
B Cell ◽  
Unfolded Protein Response ◽  
Cell Fate ◽  
Cell Receptor ◽  
B Cell Receptor ◽  
Unfolded Protein ◽  
Protein Response

scholarly journals Activation of an Unfolded Protein Response during Differentiation of Antibody-secreting B Cells

2002 ◽  
Vol 277 (50) ◽  
pp. 49047-49054 ◽  
Author(s):  
Jennifer N. Gass ◽  
Nicole M. Gifford ◽  
Joseph W. Brewer
Keyword(s):  
B Cells ◽  
Unfolded Protein Response ◽  
Unfolded Protein ◽  
Protein Response

scholarly journals The LMP1 oncogene of EBV activates PERK and the unfolded protein response to drive its own synthesis

Blood ◽  
2008 ◽  
Vol 111 (4) ◽  
pp. 2280-2289 ◽  
Author(s):  
Dong Yun Lee ◽  
Bill Sugden
Keyword(s):  
B Cells ◽  
Unfolded Protein Response ◽  
Threshold Level ◽  
Initiation Factor ◽  
Barr Virus ◽  
Unfolded Protein ◽  
General Protein Synthesis ◽  
Epstein Barr ◽  
The Unfolded Protein Response ◽  
Protein Response

The oncogene latent membrane protein 1 (LMP1) of Epstein-Barr virus (EBV) without a ligand drives proliferation of EBV-infected B cells. Its levels vary in cells of clonal populations by more than 100-fold, which leads to multiple distinct activities of the oncogene. At intermediate levels it drives proliferation, and at high levels it inhibits general protein synthesis by inducing phosphorylation of eukaryotic initiation factor 2α (eIF2α). We have found that LMP1 activates PERK to induce phosphorylation of eIF2α, which upregulates activating transcription factor 4 (ATF4) expression. ATF4, in turn, transactivates LMP1's own promoter. LMP1 activates not only PERK but also inositol requiring kinase 1 (IRE1) and ATF6, 3 pathways of the unfolded protein response (UPR). Increasing expression levels of LMP1 induced a dose-dependent increase in IRE1 activity, as measured by its “splicing” of XBP-1. These infected B cells secrete immunoglobins independent of the levels of LMP1, indicating that only a threshold level of XBP-1 is required for the secretion. These findings indicate that LMP1's activation of the UPR is a normal event in a continuum of LMP1's expression that leads both to stimulatory and inhibitory functions and regulates the physiology of EBV-infected B cells in multiple, unexpected modes.

scholarly journals Retrotransposon derepression leads to activation of the unfolded protein response and apoptosis in pro-B cells

Development ◽  
2016 ◽  
Vol 143 (10) ◽  
pp. 1788-1799 ◽  
Author(s):  
Alessandra Pasquarella ◽  
Anja Ebert ◽  
Gustavo Pereira de Almeida ◽  
Maria Hinterberger ◽  
Maryam Kazerani ◽  
...  
Keyword(s):  
B Cells ◽  
Unfolded Protein Response ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response
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