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Biochemistry Research International
Volume 2012, Article ID 738471, 7 pages
Review Article

UPR-Mediated Membrane Biogenesis in B Cells

1Department of Microbiology and Immunology, College of Medicine, University of South Alabama, Mobile, AL 36688, USA
2Department of Infectious Diseases, St. Jude Children's Research Hospital, Memphis, TN 38105, USA

Received 5 August 2011; Accepted 25 August 2011

Academic Editor: Kezhong Zhang

Copyright © 2012 Joseph W. Brewer and Suzanne Jackowski. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


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.