{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T02:19:18Z","timestamp":1792721958684,"version":"4.5.0"},"reference-count":51,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2010,12,29]],"date-time":"2010-12-29T00:00:00Z","timestamp":1293580800000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Eur J Immunol"],"published-print":{"date-parts":[[2011,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:p>Plasma cells (PCs) secrete copious levels of immunoglobulins. To achieve this, their endoplasmic reticulum (ER) undergoes expansion in a process that requires continuous ER stress and activation of the unfolded protein response. It is important that protein synthesis, the driver of ER stress, is regulated in a manner that does not induce apoptosis. We followed protein synthesis in murine splenic B cells activated in vitro with LPS. Total protein synthesis levels increased and then steeply decreased when the cells acquired a secretory phenotype. We explored the involvement of two mechanisms in controlling protein synthesis levels, namely ER stress\u2010mediated phosphorylation of eukaryote initiation factor 2\u03b1 (eIF2\u03b1) and the mammalian target of rapamycin (mTOR) pathway, which attenuate or activate mRNA translation, respectively. We show that induction of ER stress in activated B cells counter\u2010intuitively led to dephosphorylation of eIF2\u03b1. Despite the reduction in phosphorylated eIF2\u03b1, expression of activating transcription factor 4, an effector of hyper eIF2\u03b1 phosphorylation, was induced. In addition, ER stress attenuated the mTOR pathway, which ultimately reduced protein synthesis. Finally, B cells engineered to overactivate the mTOR pathway exhibited higher apoptosis in the course of LPS stimulation. We conclude that protein synthesis in PCs is controlled by an ER stress\u2010mediated mTOR regulation, which is needed for optimal cell viability.<\/jats:p>","DOI":"10.1002\/eji.201040677","type":"journal-article","created":{"date-parts":[[2010,12,6]],"date-time":"2010-12-06T07:52:21Z","timestamp":1291621941000},"page":"491-502","source":"Crossref","is-referenced-by-count":56,"title":["Protein synthesis in plasma cells is regulated by crosstalk between endoplasmic reticulum stress and mTOR signaling"],"prefix":"10.1002","volume":"41","author":[{"given":"Meidan","family":"Goldfinger","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Miri","family":"Shmuel","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sandrine","family":"Benhamron","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Boaz","family":"Tirosh","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"311","published-online":{"date-parts":[[2010,12,29]]},"reference":[{"key":"e_1_2_6_2_2","doi-asserted-by":"publisher","DOI":"10.1146\/annurev.immunol.21.120601.141138"},{"key":"e_1_2_6_3_2","doi-asserted-by":"publisher","DOI":"10.1038\/ni1357"},{"key":"e_1_2_6_4_2","doi-asserted-by":"publisher","DOI":"10.1016\/0092-8674(94)90321-2"},{"key":"e_1_2_6_5_2","doi-asserted-by":"publisher","DOI":"10.1038\/35085509"},{"key":"e_1_2_6_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.immuni.2004.06.010"},{"key":"e_1_2_6_7_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M205011200"},{"key":"e_1_2_6_8_2","doi-asserted-by":"publisher","DOI":"10.1038\/ni907"},{"key":"e_1_2_6_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/nrm2199"},{"key":"e_1_2_6_10_2","doi-asserted-by":"publisher","DOI":"10.1074\/jbc.M405616200"},{"key":"e_1_2_6_11_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.153.5.1011"},{"key":"e_1_2_6_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(01)00611-0"},{"key":"e_1_2_6_13_2","doi-asserted-by":"publisher","DOI":"10.1038\/415092a"},{"key":"e_1_2_6_14_2","doi-asserted-by":"publisher","DOI":"10.1084\/jem.20050575"},{"key":"e_1_2_6_15_2","doi-asserted-by":"publisher","DOI":"10.1038\/emboj.2009.117"},{"key":"e_1_2_6_16_2","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.0900953"},{"key":"e_1_2_6_17_2","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.0802990"},{"key":"e_1_2_6_18_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molimm.2007.07.029"},{"key":"e_1_2_6_19_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1097-2765(03)00105-9"},{"key":"e_1_2_6_20_2","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/19.5.1087"},{"key":"e_1_2_6_21_2","doi-asserted-by":"publisher","DOI":"10.1038\/sj.onc.1209889"},{"key":"e_1_2_6_22_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80125-7"},{"key":"e_1_2_6_23_2","doi-asserted-by":"publisher","DOI":"10.1101\/gad.12.4.502"},{"key":"e_1_2_6_24_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ccr.2010.01.021"},{"key":"e_1_2_6_25_2","doi-asserted-by":"publisher","DOI":"10.4049\/jimmunol.177.6.3791"},{"key":"e_1_2_6_26_2","doi-asserted-by":"publisher","DOI":"10.1002\/eji.200737281"},{"key":"e_1_2_6_27_2","doi-asserted-by":"publisher","DOI":"10.1093\/emboj\/cdg112"},{"key":"e_1_2_6_28_2","doi-asserted-by":"publisher","DOI":"10.1182\/blood-2007-03-077222"},{"key":"e_1_2_6_29_2","doi-asserted-by":"publisher","DOI":"10.1016\/S1074-7613(94)80022-7"},{"key":"e_1_2_6_30_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0092-8674(00)80373-6"},{"key":"e_1_2_6_31_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cmet.2008.01.008"},{"key":"e_1_2_6_32_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1101902"},{"key":"e_1_2_6_33_2","first-page":"475","article-title":"GADD34 inhibits mammalian target of rapamycin signaling via tuberous sclerosis complex and controls cell survival under bioenergetic stress","volume":"19","author":"Watanabe R.","year":"2007","journal-title":"Int. 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