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J. Biol. Chem., Vol. 275, Issue 22, 16466-16472, June 2, 2000

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IB1 Reduces Cytokine-induced Apoptosis of Insulin-secreting Cells^*

Christophe Bonny^§¶, Anne Oberson, Myriam Steinmann, Daniel F. Schorderet, Pascal Nicod, and Gérard Waeber^§

From the  Division of Medical Genetics and the  Department of Internal Medicine, CHUV University Hospital, 1011 Lausanne Switzerland

IB1/JIP-1 is a scaffold protein that interacts with upstream components of the c-Jun N-terminal kinase (JNK) signaling pathway. IB1 is expressed at high levels in pancreatic  cells and may therefore exert a tight control on signaling events mediated by JNK in these cells. Activation of JNK by interleukin 1 (IL-1) or by the upstream JNK constitutive activator MEKK1 promoted apoptosis in two pancreatic  cell lines and decreased IB1 content by 50-60%. To study the functional consequences of the reduced IB1 content in  cell lines, we used an insulin-secreting cell line expressing an inducible IB1 antisense RNA that lead to a 38% IB1 decrease. Reducing IB1 levels in these cells increased phosphorylation of c-Jun and increased the apoptotic rate in presence of IL-1. Nitric oxide production was not stimulated by expression of the IB1 antisense RNA. Complementary experiments indicated that overexpression of IB1 in insulin-producing cells prevented JNK-mediated activation of the transcription factors c-Jun, ATF2, and Elk1 and decreased IL-1- and MEKK1-induced apoptosis. These data indicate that IB1 plays an anti-apoptotic function in insulin-producing cells probably by controlling the activity of the JNK signaling pathway.

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