| First Author | Aragon IV | Year | 2012 |
| Journal | Mol Immunol | Volume | 51 |
| Issue | 3-4 | Pages | 347-55 |
| PubMed ID | 22555069 | Mgi Jnum | J:188171 |
| Mgi Id | MGI:5439259 | Doi | 10.1016/j.molimm.2012.04.001 |
| Citation | Aragon IV, et al. (2012) The specialized unfolded protein response of B lymphocytes: ATF6alpha-independent development of antibody-secreting B cells. Mol Immunol 51(3-4):347-55 |
| abstractText | B lymphocytes, like all mammalian cells, are equipped with the unfolded protein response (UPR), a complex signaling system allowing for both pro- and mal-adaptive responses to increased demands on the endoplasmic reticulum (ER). The UPR is comprised of three signaling pathways initiated by the ER transmembrane stress sensors, IRE1alpha/beta, PERK and ATF6alpha/beta. Activation of IRE1 yields XBP1(S), a transcription factor that directs expansion of the ER and enhances protein biosynthetic and secretory machinery. XBP1(S) is essential for the differentiation of B lymphocytes into antibody-secreting cells. In contrast, the PERK pathway, a regulator of translation and transcription, is dispensable for the generation of antibody-secreting cells. Functioning as a transcription factor, ATF6alpha can augment ER quality control processes and drive ER expansion, but the potential role of this UPR pathway in activated B cells has not been investigated. Here, we report studies of ATF6alpha-deficient B cells demonstrating that ATF6alpha is not required for the development of antibody-secreting cells. Thus, when B cells are stimulated to secrete antibody, a specialized UPR relies exclusively on the IRE1-XBP1 pathway to remodel the ER and expand cellular secretory capacity. |
