UPR-Mediated Membrane Biogenesis in B Cells
The unfolded protein response (UPR) can coordinate the regulation of gene transcription and protein translation to balance the load of client proteins with the protein folding and degradative capacities of...
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Format: | Article |
Language: | English |
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Wiley
2012-01-01
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Series: | Biochemistry Research International |
Online Access: | http://dx.doi.org/10.1155/2012/738471 |
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author | Joseph W. Brewer Suzanne Jackowski |
author_facet | Joseph W. Brewer Suzanne Jackowski |
author_sort | Joseph W. Brewer |
collection | DOAJ |
description | The unfolded protein
response (UPR) can coordinate the regulation of
gene transcription and protein translation to
balance the load of client proteins with the
protein folding and degradative capacities of
the ER. Increasing evidence also implicates the
UPR in the regulation of lipid synthesis and
membrane biogenesis. The differentiation of
B lymphocytes into antibody-secreting cells is
marked by significant expansion of the ER, the
site for antibody synthesis and assembly. In
activated B cells, the demand for membrane
protein and lipid components leads to activation
of the UPR transcriptional activator XBP1(S)
which, in turn, initiates a cascade of
biochemical events that enhance supplies of
phospholipid precursors and build machinery for
the synthesis, maturation, and transport of
secretory proteins. The alterations in lipid
metabolism that occur during this developmental
transition and the impact of membrane
phospholipid restriction on B cell secretory
characteristics are discussed in this
paper. |
format | Article |
id | doaj-art-600d4470c0924b1aaa898907b6ec7618 |
institution | Kabale University |
issn | 2090-2247 2090-2255 |
language | English |
publishDate | 2012-01-01 |
publisher | Wiley |
record_format | Article |
series | Biochemistry Research International |
spelling | doaj-art-600d4470c0924b1aaa898907b6ec76182025-02-03T01:11:17ZengWileyBiochemistry Research International2090-22472090-22552012-01-01201210.1155/2012/738471738471UPR-Mediated Membrane Biogenesis in B CellsJoseph W. Brewer0Suzanne Jackowski1Department of Microbiology and Immunology, College of Medicine, University of South Alabama, Mobile, AL 36688, USADepartment of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, TN 38105, USAThe unfolded protein response (UPR) can coordinate the regulation of gene transcription and protein translation to balance the load of client proteins with the protein folding and degradative capacities of the ER. Increasing evidence also implicates the UPR in the regulation of lipid synthesis and membrane biogenesis. The differentiation of B lymphocytes into antibody-secreting cells is marked by significant expansion of the ER, the site for antibody synthesis and assembly. In activated B cells, the demand for membrane protein and lipid components leads to activation of the UPR transcriptional activator XBP1(S) which, in turn, initiates a cascade of biochemical events that enhance supplies of phospholipid precursors and build machinery for the synthesis, maturation, and transport of secretory proteins. The alterations in lipid metabolism that occur during this developmental transition and the impact of membrane phospholipid restriction on B cell secretory characteristics are discussed in this paper.http://dx.doi.org/10.1155/2012/738471 |
spellingShingle | Joseph W. Brewer Suzanne Jackowski UPR-Mediated Membrane Biogenesis in B Cells Biochemistry Research International |
title | UPR-Mediated Membrane Biogenesis in B Cells |
title_full | UPR-Mediated Membrane Biogenesis in B Cells |
title_fullStr | UPR-Mediated Membrane Biogenesis in B Cells |
title_full_unstemmed | UPR-Mediated Membrane Biogenesis in B Cells |
title_short | UPR-Mediated Membrane Biogenesis in B Cells |
title_sort | upr mediated membrane biogenesis in b cells |
url | http://dx.doi.org/10.1155/2012/738471 |
work_keys_str_mv | AT josephwbrewer uprmediatedmembranebiogenesisinbcells AT suzannejackowski uprmediatedmembranebiogenesisinbcells |