Stress‐mediated apoptosis may play a crucial role in loss of pancreatic β‐cell mass, contributing to the development of diabetes. We have recently identified that translational control involving the translational suppressor eIF4E binding protein‐1 (4E‐BP1) which is important for β‐cell survival under endoplasmic reticulum (ER) stress. The Eif4ebp1 gene, encoding 4E‐BP1, is a direct target of a transcription factor activating transcription factor‐4 (ATF4), a master regulator of gene expression in stress responses. In the current study, we investigated 4E‐BP1 expression in mouse insulinoma line 6 (MIN6) cells treated with arsenite, an inducer of oxidative stress which is another contributor of β‐cell loss. We found that arsenite‐induced 4E‐BP1 expression level was lower than that induced by thapsigargin, an ER stress inducer, although ATF4 was similarly induced by these agents. The ratio of the dephosphorylated form of 4E‐BP1, which has the highest activity, to phosphorylated forms was, however, greater in MIN6 cells treated with arsenite as compared to that in thapsigargin‐treated cells. Arsenite‐induced 4E‐BP1 mRNA and protein expressions were augmented by simultaneous treatment with a c‐Jun N‐terminal kinase (JNK) specific inhibitor, SP600125. The agent also suppressed the level of the dephosphrylated form of 4E‐BP1 in arsenite‐treated MIN6 cells. Thus, JNK activated by oxidative stress is involved in the modulation of 4E‐BP1 expression and phosphorylation in MIN6 cells, which may contribute to fine tuning of translational control under stress conditions. Copyright © 2010 John Wiley & Sons, Ltd.